SS-31 10MG
$34.00
Technical Specifications
- Product Name: SS-31 10MG
- Scientific Name: Elamipretide
- Common Name: SS-31
- Peptide Classification: Synthetic Mitochondria-Targeted Tetrapeptide
- Primary Research Areas: Cardiolipin-Associated Membrane Systems, Inner Mitochondrial Membrane Biology, Oxidative Phosphorylation, Electron-Transport-Chain Research, and Cellular Bioenergetics
- Amino Acid Sequence: D-Arg-Dmt-Lys-Phe-NH2
- Molecular Formula: C32H49N9O5
- Molecular Weight: Approximately 639.8 g/mol
- CAS Number: 736992-21-5
- PubChem CID: 11764719
- Appearance: White to Off-White Lyophilized Powder
- Research Quantity: 10MG
- Intended Use: Laboratory Research Only
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Standardized research quantity for mitochondrial, cardiolipin and analytical peptide studies
Four-residue Szeto–Schiller peptide represented as D-Arg-Dmt-Lys-Phe-NH₂
Investigated in inner mitochondrial membrane, cristae and oxidative-phosphorylation models
Prepared and shipped from our Texas facility with fast U.S. order processing
A defined lyophilized research format containing 10MG of SS-31, also known in scientific literature as elamipretide, MTP-131 and Bendavia. SS-31 is a synthetic aromatic-cationic tetrapeptide investigated in controlled laboratory systems involving cardiolipin interaction, inner mitochondrial membrane organization, cristae structure, electron-transport-chain efficiency, oxidative phosphorylation, mitochondrial respiration, reactive-species biology and cellular bioenergetics.
SS-31 10MG Research Summary
SS-31 is a synthetic, mitochondria-targeted tetrapeptide belonging to the Szeto–Schiller peptide family.
It is commonly represented by the sequence D-Arg-Dmt-Lys-Phe-NHâ‚‚, where Dmt identifies the nonstandard aromatic amino-acid residue 2,6-dimethyltyrosine.
The sequence contains four amino-acid residues and a C-terminal amide.
SS-31 is also widely identified in scientific literature as elamipretide, MTP-131 and Bendavia.
The peptide is investigated for its ability to concentrate within mitochondria without requiring the large membrane-potential-dependent accumulation associated with conventional lipophilic cations.
Its alternating aromatic and basic structural pattern contributes to interaction with biological membranes and negatively charged phospholipids.
A primary research focus is cardiolipin, a negatively charged phospholipid enriched within the inner mitochondrial membrane.
Cardiolipin supports membrane curvature, cristae organization, respiratory-chain protein interactions and mitochondrial bioenergetics.
Published research has examined SS-31 interaction with cardiolipin through electrostatic and hydrophobic forces.
SS-31 has also been investigated in relation to the cytochrome c–cardiolipin complex, electron-transfer function, cardiolipin oxidation and mitochondrial cristae integrity.
Additional experimental systems have evaluated mitochondrial respiration, ATP production, proton leak, membrane potential, reactive oxygen species, mitochondrial permeability, apoptosis-associated signaling and cellular stress.
SS-31 is not a mitochondrial-derived peptide. Unlike MOTS-c and humanin, it is a deliberately designed synthetic peptide rather than a sequence identified from a mitochondrial open reading frame.
SS-31 is not a conventional antioxidant molecule that functions solely through nonspecific free-radical scavenging.
Its reported effects are investigated primarily in the context of mitochondrial membrane organization, cardiolipin-associated protein function and bioenergetic efficiency.
The 10MG format may support pilot mitochondrial assays, concentration-response studies, respiration experiments, cardiolipin-binding research, analytical method development and stability testing.
SS-31 10MG is supplied exclusively for controlled laboratory research. It is not represented as a pharmaceutical or prescription product and is not intended for human or veterinary administration.
Technical Specifications
SS-31 10MG
Elamipretide
SS-31, MTP-131 and Bendavia
Synthetic mitochondria-targeted tetrapeptide
Szeto–Schiller peptide
10MG per vial
Lyophilized research material
Four amino-acid residues
D-Arg-Dmt-Lys-Phe-NHâ‚‚
2,6-Dimethyltyrosine
D-Arginine
Phenylalaninamide
C32H49N9O5
Approximately 639.8 g/mol
736992-21-5
11764719
Alternating aromatic and basic residues
Aromatic-cationic peptide
Cardiolipin-associated inner mitochondrial membrane systems
Mitochondrial structure, respiration, ATP production and oxidative stress
HPLC, LC-MS, peptide mapping and stability analysis
Refer to available lot-specific analytical documentation
Laboratory research only
The formula and molecular weight above describe the commonly referenced free-base molecular form. Hydrochloride, acetate, trifluoroacetate, hydration or other material forms may have different total formula weights. Researchers should consult lot-specific documentation when performing quantitative calculations.
Peptide Sequence and Structural Identity
D-Arg-Dmt-Lys-Phe-NHâ‚‚
Residue Description:
D-Arginine–2,6-Dimethyltyrosine–Lysine–Phenylalaninamide
SS-31 is a compact tetrapeptide with a deliberately engineered alternating aromatic-cationic architecture.
The basic residues D-arginine and lysine contribute positive charge under many experimental conditions.
The aromatic residues 2,6-dimethyltyrosine and phenylalanine contribute hydrophobic and aromatic interactions.
This alternating pattern is an important feature of Szeto–Schiller peptides.
D-arginine differs stereochemically from naturally occurring L-arginine and may influence enzymatic stability.
The Dmt residue is a modified tyrosine containing methyl groups at the 2 and 6 positions of the aromatic ring.
Dmt contributes aromaticity and contains a phenolic hydroxyl group.
The C-terminal amide distinguishes SS-31 from a peptide containing a free C-terminal carboxyl group.
Removal of the terminal amide, substitution of D-arginine, alteration of Dmt or sequence scrambling would create a chemically distinct peptide.
SS-31 contains no cysteine residues and does not require a conventional disulfide bridge.
Provides a positively charged guanidinium-containing residue with nonstandard stereochemistry.
Provides an aromatic phenolic residue modified by two methyl groups.
Contributes a positively charged amino side chain under many experimental conditions.
Provides the terminal aromatic residue and a C-terminal amide structure.
Alternating aromatic and basic residues contribute to membrane-associated behavior.
The four-residue sequence contains no cysteine and no conventional disulfide connectivity.
Molecular Characteristics of SS-31
SS-31 is substantially smaller than many conventional signaling peptides.
Its molecular weight is approximately 639.8 g/mol in the referenced free-base form.
The molecule contains both positively charged and hydrophobic structural features.
This combination supports interaction with negatively charged phospholipid membranes while maintaining a compact peptide structure.
SS-31 is water-associated as a peptide but may also display strong membrane interactions because of its aromatic residues.
The molecule does not contain a long hydrophobic alkyl chain and is not classified as a lipidated peptide.
Its mitochondrial localization should not be interpreted as equivalent to the mechanism used by triphenylphosphonium-linked compounds.
SS-31 may produce singly, doubly or multiply charged ions during electrospray-ionization mass spectrometry depending on source conditions and pH.
Analytical interpretation should distinguish intact SS-31 from terminally modified, oxidized, hydrolyzed, truncated or adduct-associated species.
SS-31 contains only four residues while retaining distinct membrane-associated properties.
D-arginine and lysine contribute positive charge.
Dmt and phenylalanine contribute aromatic interactions.
Amidation forms part of the compound’s defined structural identity.
SS-31 targets mitochondrial membranes without conventional peptide lipidation.
The sequence does not contain cysteine residues.
Electrostatic and aromatic interactions may contribute to phospholipid binding.
Changes in residue order, stereochemistry or terminal chemistry create distinct compounds.
Scientific Background
SS-31 emerged from research into short aromatic-cationic peptides capable of crossing cellular membranes and concentrating within mitochondria.
These compounds became known as Szeto–Schiller peptides.
Early research evaluated the relationship between alternating aromatic and basic residues, mitochondrial localization and oxidative-stress-associated responses.
Subsequent studies focused increasingly on cardiolipin and inner mitochondrial membrane structure.
Cardiolipin is a structurally unusual phospholipid containing four fatty-acid chains and two phosphate groups.
Its negative charge and membrane distribution contribute to interaction with numerous mitochondrial proteins.
SS-31 has been investigated as a cardiolipin-interacting compound capable of modifying the local membrane environment.
Research models have examined how that interaction may influence cristae architecture, respiratory-chain organization, cytochrome c behavior and ATP synthesis.
Findings span biochemical, cellular, isolated mitochondrial, tissue and animal research systems.
Results from one model should not automatically be generalized to every tissue, species or experimental condition.
Szeto–Schiller Peptide Research
Szeto–Schiller peptides are short synthetic peptides characterized by alternating aromatic and basic amino-acid residues.
Members of the family differ in sequence, stereochemistry, terminal structure and experimental activity.
SS-31 is among the most extensively investigated members of this peptide class.
The peptide family was developed through structure–activity research rather than discovery from an endogenous genomic sequence.
Aromatic residues may contribute hydrophobic interactions with membrane lipids.
Basic residues may contribute electrostatic interaction with negatively charged phospholipid head groups.
D-amino-acid incorporation may alter resistance to selected proteolytic enzymes.
Closely related sequence variants should not be treated as analytically or biologically interchangeable.
Cardiolipin Biology
Cardiolipin is a phospholipid enriched within the inner mitochondrial membrane.
Its molecular structure supports membrane curvature and interaction with proteins involved in respiration, substrate transport and mitochondrial dynamics.
Cardiolipin is particularly concentrated in mitochondrial cristae.
It may stabilize individual respiratory complexes and larger respiratory-chain supercomplexes.
Cardiolipin also interacts with cytochrome c, an electron carrier located within the mitochondrial intermembrane space.
Oxidation, depletion or abnormal remodeling of cardiolipin may alter mitochondrial membrane structure and protein function.
SS-31 is investigated for reversible interaction with cardiolipin through electrostatic and hydrophobic forces.
Cardiolipin binding should be distinguished from irreversible covalent modification.
Experimental methods may include liposome binding, fluorescence spectroscopy, calorimetry, nuclear magnetic resonance and membrane-partitioning analysis.
Inner Mitochondrial Membrane Research
The inner mitochondrial membrane separates the mitochondrial matrix from the intermembrane space.
It contains the respiratory-chain complexes, ATP synthase, metabolite transporters and additional proteins required for mitochondrial function.
The membrane is extensively folded into cristae, increasing available surface area for oxidative phosphorylation.
Inner-membrane lipid composition influences curvature, protein organization and proton handling.
Cardiolipin represents an important structural and functional component of this membrane.
SS-31 research frequently evaluates membrane organization, fluidity, protein interaction and resistance to structural disruption.
Measurements of membrane-associated function should be interpreted alongside mitochondrial quantity and sample integrity.
Mitochondrial Cristae Research
Cristae are folds of the inner mitochondrial membrane.
Their shape, density and junction organization influence the distribution of respiratory proteins and ATP synthase.
Cristae structure may change during energetic stress, aging, inflammation, ischemia, genetic mitochondrial dysfunction and cell-death signaling.
SS-31 has been investigated for its relationship with cardiolipin-dependent cristae organization.
Electron microscopy and electron tomography may be used to evaluate cristae density, width, curvature and junction structure.
Changes in cristae morphology should not be interpreted without functional respiration and membrane-integrity data.
Mitochondrial shape and cristae shape represent related but distinct structural measurements.
Electron-Transport-Chain Research
The mitochondrial electron-transport chain transfers electrons through a series of protein complexes within the inner mitochondrial membrane.
Complexes I, III and IV contribute to proton translocation across the membrane.
The resulting electrochemical gradient supports ATP synthesis by complex V.
Cardiolipin interacts with respiratory-chain proteins and may support their organization and stability.
SS-31 research may evaluate complex activity, electron transfer, oxygen consumption and respiratory-control ratios.
Increased oxygen consumption does not independently establish improved coupling or increased ATP production.
Respiration should be interpreted alongside proton leak, membrane potential, ATP synthesis and substrate availability.
Evaluation of NADH-linked electron transfer and associated respiration.
Evaluation of succinate-linked electron entry into the respiratory chain.
Investigation of ubiquinol oxidation and cytochrome c reduction.
Evaluation of cytochrome c oxidation and oxygen reduction.
Investigation of proton-gradient-driven ATP synthesis.
Evaluation of higher-order organization among electron-transport-chain complexes.
Cytochrome c and Cardiolipin Research
Cytochrome c is a small heme-containing protein located within the mitochondrial intermembrane space.
Under normal respiratory conditions, it transfers electrons between complex III and complex IV.
Cytochrome c may also interact with cardiolipin.
Under selected stress conditions, the cytochrome c–cardiolipin complex may display peroxidase-associated behavior.
This process has been investigated in relation to cardiolipin oxidation and apoptosis-associated mitochondrial signaling.
SS-31 has been studied for its capacity to alter the cytochrome c–cardiolipin interaction while preserving electron-carrier function.
Potential endpoints include cytochrome c peroxidase activity, cardiolipin oxidation, electron transfer and cytochrome c release.
Reduced cytochrome c release does not independently establish that every upstream or downstream cell-death pathway has been inhibited.
Oxidative-Phosphorylation Research
Oxidative phosphorylation couples respiratory-chain electron transfer with ATP synthesis.
Its efficiency depends on substrate availability, respiratory-complex function, membrane integrity, proton conductance and ATP synthase activity.
SS-31 has been investigated in systems involving mitochondrial coupling and ATP-generating capacity.
Potential measurements include oxygen consumption, ATP production, phosphate-to-oxygen ratio and respiratory-control ratio.
Increased respiration may represent productive ATP synthesis, compensatory energy demand or uncoupled oxygen consumption.
Multiple measurements are therefore required to characterize oxidative-phosphorylation efficiency.
Results may differ among isolated mitochondria, permeabilized cells, intact cells and whole tissues.
ATP-Production Research
Adenosine triphosphate is a central cellular energy-transfer molecule.
Mitochondrial ATP production depends on the proton-motive force, ATP synthase and transport of adenine nucleotides across the inner membrane.
SS-31 research may evaluate total ATP, mitochondrial ATP production and ATP-production rate.
Total cellular ATP may also reflect glycolytic contribution.
A stable ATP concentration does not necessarily indicate an unchanged ATP-production rate because production and consumption may change together.
Luciferase-based ATP assays should include controls for direct peptide interference.
ATP measurements may be strengthened by simultaneous respiration, membrane-potential and metabolomic analysis.
Adenine-Nucleotide-Transport Research
Adenine nucleotide translocase exchanges mitochondrial ATP for cytosolic ADP across the inner mitochondrial membrane.
This transport process is required for efficient coupling between mitochondrial ATP production and cellular energy use.
Published research has investigated interaction between elamipretide and adenine nucleotide translocase-associated systems.
Experimental endpoints may include ADP sensitivity, nucleotide transport, respiratory kinetics and protein-interaction mapping.
Direct protein interaction should be distinguished from indirect changes caused by cardiolipin or membrane organization.
Genetic, biochemical and structural methods may provide complementary evidence.
Mitochondrial Membrane-Potential Research
The mitochondrial membrane potential is an electrical component of the proton-motive force.
It arises from respiratory-chain proton translocation across the inner mitochondrial membrane.
Membrane potential supports ATP synthesis, metabolite transport and mitochondrial protein import.
Excessive depolarization may indicate respiratory dysfunction or membrane permeabilization.
Excessive hyperpolarization may also accompany selected stress conditions.
SS-31 research may measure membrane potential using fluorescent probes or electrode-based methods.
Probe accumulation depends on mitochondrial mass, plasma-membrane potential, loading conditions and dye concentration.
Membrane-potential data should therefore be normalized and supported by appropriate positive and negative controls.
Proton-Leak and Coupling Research
Proton leak describes movement of protons across the inner mitochondrial membrane without productive ATP synthesis.
Some proton conductance is physiological, while excessive leak may reduce bioenergetic efficiency.
Membrane lipid organization, uncoupling proteins and membrane damage may influence proton leak.
Cardiolipin contributes to the organization of the inner mitochondrial membrane and local proton environment.
SS-31 has been investigated in relation to mitochondrial coupling and membrane-associated energetic efficiency.
Proton leak may be estimated through respiration measurements after inhibition of ATP synthase.
Interpretation should account for mitochondrial content, substrate supply and membrane integrity.
Reactive Oxygen Species Research
Reactive oxygen species are generated during normal metabolism and may participate in signaling.
Excessive or poorly controlled reactive-species production may modify lipids, proteins and nucleic acids.
Respiratory-chain inefficiency can increase electron leakage and reactive-species formation under selected conditions.
Cardiolipin is susceptible to oxidative modification because of its fatty-acid composition and mitochondrial location.
SS-31 research may evaluate superoxide-associated probes, hydrogen-peroxide measurements, oxidized lipids and protein oxidation.
Reduced probe signal does not independently demonstrate direct radical scavenging.
A lower signal may instead reflect altered electron transport, membrane organization, probe uptake or cellular viability.
Cell-free interference controls and orthogonal oxidative-damage markers are recommended.
Oxidative-Stress Research
Oxidative stress describes an imbalance between reactive molecular species and cellular protective systems.
Mitochondrial oxidative stress may involve respiratory-chain dysfunction, cardiolipin oxidation, altered antioxidant systems and damage to mitochondrial DNA.
SS-31 has been investigated in models involving chemically induced oxidative stress, ischemia-reperfusion, metabolic stress and aging.
Potential endpoints include lipid peroxidation, protein carbonyls, oxidized cardiolipin, glutathione status and antioxidant-enzyme activity.
One oxidative marker should not be treated as a complete measure of cellular redox state.
Timing matters because reactive-species production and oxidative damage may occur at different stages.
Experimental systems should distinguish prevention of oxidative damage from repair of established molecular damage.
Mitochondrial Permeability Research
Mitochondrial membrane permeabilization is associated with severe energetic stress and cell-death signaling.
The permeability transition may involve loss of membrane potential, mitochondrial swelling and release of intermembrane-space proteins.
Cardiolipin oxidation and membrane disorganization may contribute to these processes.
SS-31 may be studied through mitochondrial swelling, calcium-retention capacity, membrane-potential and cytochrome c-release assays.
Permeability-transition measurements vary substantially among isolated organelles, permeabilized cells and intact cells.
Appropriate positive controls should confirm that the assay can detect mitochondrial permeabilization.
Apoptosis-Associated Research
Mitochondria participate in intrinsic apoptosis through membrane permeabilization and release of signaling proteins.
Cytochrome c release may promote formation of the apoptosome and activation of downstream caspases.
SS-31 research has examined mitochondrial events associated with cellular injury and apoptosis.
Potential endpoints include cytochrome c localization, caspase activation, phosphatidylserine exposure and DNA fragmentation.
Reduced caspase activity does not independently establish preservation of mitochondrial function.
Likewise, improved mitochondrial measurements do not independently establish complete inhibition of cell death.
Viability and death-pathway assays should be interpreted together.
Mitochondrial-Dynamics Research
Mitochondria continuously undergo fission, fusion, transport and structural remodeling.
These processes influence mitochondrial distribution, quality control and response to cellular stress.
Inner-membrane structure and cardiolipin biology interact with broader mitochondrial-dynamics pathways.
SS-31 research may evaluate mitochondrial length, branching, network connectivity and expression of fission- or fusion-associated proteins.
Mitochondrial morphology should not be used as a substitute for direct respiration or ATP measurements.
Image-analysis methods should define segmentation thresholds and account for cell size and mitochondrial mass.
Mitophagy and Quality-Control Research
Mitophagy is the selective degradation of damaged or unnecessary mitochondria.
It contributes to mitochondrial quality control and cellular adaptation.
Membrane depolarization, protein accumulation and oxidative damage may influence mitophagy signaling.
SS-31 may be investigated in experimental systems involving mitochondrial turnover and autophagic flux.
Measurements may include PINK1, Parkin, LC3, lysosomal colocalization and mitochondrial-content markers.
Static abundance of an autophagy marker does not independently establish increased or decreased flux.
Flux experiments should include lysosomal inhibition or other validated methods.
Mitochondrial-Biogenesis Research
Mitochondrial biogenesis involves coordinated expression of nuclear and mitochondrial genes.
It may be influenced by energy demand, AMPK, PGC-1α and additional transcriptional regulators.
SS-31 is primarily investigated for mitochondrial membrane and bioenergetic effects rather than as a direct transcriptional agonist.
Nevertheless, improved mitochondrial function may interact with adaptive gene-expression programs.
Potential endpoints include mitochondrial DNA copy number, respiratory-protein abundance, PGC-1α and citrate-synthase activity.
Increased mitochondrial content should be distinguished from improved function of existing mitochondria.
Cellular-Bioenergetics Research
Cellular bioenergetics reflects the balance among energy production, energy consumption and substrate availability.
SS-31 may be studied through oxygen-consumption rate, extracellular acidification, ATP production and metabolite analysis.
Basal respiration, ATP-linked respiration, proton leak, maximal respiration and spare respiratory capacity represent separate endpoints.
Glycolytic activity may compensate when mitochondrial ATP production is impaired.
Intact-cell measurements integrate mitochondrial function with transport, signaling and cellular demand.
Isolated-mitochondria experiments provide greater control but remove important cellular context.
Parallel use of several model types may provide stronger mechanistic interpretation.
Ischemia–Reperfusion Research
Ischemia restricts oxygen and nutrient delivery to tissue.
Reperfusion restores circulation but may produce rapid ionic, metabolic and oxidative changes.
Mitochondrial dysfunction is a major feature of many ischemia–reperfusion models.
SS-31 has been investigated in cellular, organ and animal models involving ischemia followed by reperfusion.
Potential endpoints include respiration, infarct-associated tissue damage, cardiolipin oxidation, reactive species, ATP and cell viability.
Results may differ according to tissue type, ischemic duration, reperfusion duration and timing of experimental exposure.
Findings from preclinical ischemia–reperfusion models do not establish safety or efficacy in humans.
Cardiac Mitochondrial Research
Cardiac tissue contains dense mitochondrial populations and provides a high-energy-demand model for studying mitochondrial biology.
SS-31 has been investigated in cardiac experimental systems involving altered mitochondrial respiration, oxidative stress and membrane organization.
Potential laboratory endpoints include oxygen consumption, ATP-associated measurements, cardiolipin oxidation, membrane potential and mitochondrial ultrastructure.
Whole-tissue observations should be distinguished from isolated-mitochondrial measurements because vascular, electrical, mechanical and metabolic variables may influence results.
Findings from animal cardiac models do not establish safety or efficacy in humans.
Skeletal-Muscle Research
Skeletal-muscle systems provide controlled models for studying mitochondrial energy production, substrate utilization and bioenergetic adaptation.
SS-31 has been investigated in skeletal-muscle models involving altered mitochondrial function, age-associated bioenergetic changes and mitochondrial stress.
Potential laboratory endpoints include oxygen consumption, ATP-associated measurements, ADP sensitivity, mitochondrial membrane potential, respiratory capacity and mitochondrial abundance.
These measurements represent distinct experimental variables and should be interpreted with appropriate normalization for cell, tissue and mitochondrial content.
Findings from skeletal-muscle research models do not establish athletic-performance effects or suitability for human administration.
Renal Mitochondrial Research
Kidney tissues have substantial energy requirements related to filtration and active solute transport.
Mitochondrial dysfunction may influence tubular, endothelial and glomerular-cell biology.
SS-31 has been investigated in renal models involving metabolic stress, ischemia, obstruction and mitochondrial injury.
Potential endpoints include mitochondrial structure, ATP, respiration, lipid accumulation, fibrosis-associated markers and renal function.
Changes in serum or urinary markers should be interpreted alongside tissue-level measurements.
Findings from preclinical renal models do not establish safety, efficacy or suitability for human administration.
Neurobiology Research
Neurons depend heavily on mitochondrial energy production and calcium handling.
Mitochondrial dysfunction may affect synaptic activity, axonal transport and cellular survival.
SS-31 has been investigated in experimental neurobiology models involving oxidative stress, neurodegeneration and ischemic injury.
Potential endpoints include neuronal respiration, membrane potential, synaptic markers, reactive species and cell viability.
Behavioral outcomes may be influenced by motor function, motivation, sensory capacity and systemic physiology.
Molecular and behavioral endpoints should therefore be interpreted together.
Retinal and Ophthalmic Research
Retinal cells have substantial energetic demands and contain specialized mitochondrial populations.
Oxidative stress and mitochondrial dysfunction are investigated in numerous retinal and optic-nerve models.
SS-31 has been evaluated in preclinical ophthalmic systems involving retinal stress and mitochondrial impairment.
Potential endpoints include retinal structure, mitochondrial respiration, electrophysiology, reactive species and cell survival.
Ophthalmic laboratory research should not be interpreted as instructions for ocular administration.
Aging and Mitochondrial-Resilience Research
Aging-associated research frequently examines changes in mitochondrial respiration, membrane structure, substrate utilization and cellular stress responses.
Cardiolipin composition, respiratory-chain organization and mitochondrial ultrastructure may also vary across age-associated experimental systems.
SS-31 has been investigated in cellular, tissue and animal models designed to examine age-associated mitochondrial biology.
Potential laboratory endpoints include respiration, ATP-associated measurements, cardiolipin composition, oxidative-status markers, membrane organization and mitochondrial ultrastructure.
Findings from age-associated experimental models do not establish lifespan effects, clinical benefit or suitability for personal use.
Aging research should define the specific molecular, cellular or mitochondrial endpoint under investigation.
Structure–Activity Considerations
SS-31’s complete sequence, stereochemistry and terminal amidation contribute to its molecular identity.
D-arginine may influence enzymatic stability and cationic character.
Dmt contributes aromatic and phenolic properties distinct from unmodified tyrosine.
Lysine contributes a second basic side chain.
Phenylalaninamide contributes an aromatic terminal region and neutralized C-terminal structure.
Sequence scrambling may preserve gross composition while changing spatial organization and biological behavior.
Removal of one residue, changing D-arginine to L-arginine or replacing Dmt with tyrosine creates a different compound.
Equal mass comparisons among SS-31 analogues do not account for differences in molecular weight or activity.
Represents the complete D-Arg-Dmt-Lys-Phe-NHâ‚‚ sequence.
May help evaluate dependence on residue order.
May evaluate the contribution of D-arginine relative to an L-residue analogue.
May help characterize the role of the modified aromatic residue.
May evaluate the effect of C-terminal amidation on stability and activity.
May be studied through membrane systems with controlled phospholipid composition.
Potential Laboratory Research Applications
Evaluation of peptide interaction with defined cardiolipin-containing membrane systems.
Investigation of mitochondrial membrane organization and integrity.
Analysis of cristae shape, density and junction organization.
Evaluation of complexes I through V and associated electron-transfer systems.
Investigation of higher-order respiratory-protein organization.
Evaluation of electron transfer, cardiolipin interaction and peroxidase-associated activity.
Measurement of basal, ATP-linked and maximal oxygen consumption.
Evaluation of mitochondrial ATP generation and energetic efficiency.
Investigation of nonproductive proton conductance across the inner membrane.
Evaluation of mitochondrial polarization under controlled stress conditions.
Measurement of mitochondrial reactive oxygen species and oxidative modifications.
Evaluation of oxidized cardiolipin species through lipidomic methods.
Investigation of membrane swelling, depolarization and calcium-retention capacity.
Analysis of cytochrome c release, caspases and mitochondrial cell-death pathways.
Evaluation of fission, fusion and network morphology.
Investigation of mitochondrial turnover and autophagic flux.
Evaluation of mitochondrial function during oxygen restriction and restoration.
Investigation of cardiac mitochondrial energetics and contractile-associated systems.
Evaluation of respiration, ATP, ADP sensitivity and contractile-associated endpoints.
Investigation of mitochondrial function in tubular, glomerular and endothelial models.
Evaluation of neuronal mitochondrial function, oxidative stress and viability.
Investigation of mitochondrial biology in retinal and optic-system models.
Evaluation of age-related mitochondrial structure and bioenergetic changes.
Identification of mitochondrial proteins associated directly or indirectly with SS-31.
Chromatographic separation of intact SS-31 and related molecular species.
Confirmation of molecular identity, charge states and degradation products.
Monitoring of intact SS-31 under controlled environmental conditions.
Evaluation of peptide loss to containers, filters and laboratory tubing.
Why Researchers May Select SS-31 10MG
Provides a standardized nominal amount for controlled laboratory allocation.
Suitable for preliminary mitochondrial and analytical method development.
Supports evaluation across multiple controlled peptide concentrations.
May support technical and biological replication in compact study designs.
Allows allocation among respiration, ATP, membrane-potential and oxidative assays.
May be divided among HPLC, LC-MS, recovery and stability workflows.
Provides a defined peptide for phospholipid-binding and membrane studies.
Offers a compact tetrapeptide suitable for targeted analytical methods.
Supports comparison with scrambled or residue-substituted peptide controls.
Provides a mechanistically distinct comparator to MOTS-c and other metabolic compounds.
Enables focused attribution without additional peptide components.
Supports controlled laboratory storage and analytical preparation.
Experimental Design Considerations
Define the Mitochondrial Model
Identify whether the experiment uses isolated mitochondria, permeabilized cells, intact cells, tissue or an organism-level model.
Define the Primary Endpoint
Distinguish cardiolipin interaction, respiration, ATP production, oxidative stress, membrane potential and structural morphology.
Use a Concentration Series
Multiple concentrations are required to characterize response shape and identify nonspecific high-concentration effects.
Use Molar Concentrations
Molar normalization is preferable when comparing SS-31 with peptides or small molecules of different molecular weights.
Include Multiple Time Points
Immediate membrane-associated effects and delayed cellular adaptations may occur on different timelines.
Characterize Baseline Mitochondrial Health
Basal respiration, mitochondrial mass and viability should be evaluated before interpreting exposure-associated changes.
Control Substrate Availability
Respiratory responses vary with glucose, fatty acids, pyruvate, glutamine and isolated-mitochondrial substrates.
Measure Coupling
Oxygen consumption should be interpreted alongside ATP-linked respiration, proton leak and membrane potential.
Confirm Cardiolipin Dependence
Defined liposomes, altered cardiolipin models or competitive conditions may strengthen mechanistic interpretation.
Monitor Peptide Integrity
HPLC or LC-MS may confirm that intact SS-31 remains detectable during prolonged experiments.
Assess Surface Recovery
Peptide losses to tubes, filters, plates and tubing should be evaluated.
Control Fluorescent-Probe Interference
SS-31 contains aromatic residues and should be evaluated for direct effects on fluorescence-based detection.
Use Orthogonal Measurements
Structural, respiratory, biochemical and molecular endpoints may provide stronger evidence together.
Separate Protection From Repair
Experiments should distinguish pre-exposure, simultaneous exposure and post-stress exposure conditions.
Document Material Form
Quantitative calculations should identify whether the peptide is represented as free base, salt or peptide-equivalent content.
Recommended Experimental Controls
Establishes baseline behavior without peptide exposure.
Determines whether the preparation medium influences the endpoint.
Characterizes concentration-dependent responses.
Accounts for incubation duration and handling.
May help determine whether activity depends on residue order.
Supports structure–activity evaluation of Dmt, D-Arg or terminal amidation.
Supports evaluation of cardiolipin-dependent binding.
Provides a defined lipid system for peptide-interaction research.
Confirms that the assay can detect increased mitochondrial respiration.
Confirms pathway specificity and instrument responsiveness.
Supports determination of maximal respiratory capacity.
Supports estimation of ATP-linked respiration and proton leak.
Confirms membrane-potential assay performance.
Confirms that the system can detect reactive-species or damage-associated changes.
Supports investigation of electron transfer and release-associated endpoints.
Distinguishes mitochondrial responses from changes in cell number or survival.
Allows functional measurements to be normalized to mitochondrial abundance.
Determines whether SS-31 directly alters assay detection chemistry.
Identifies background from solvents, buffers, columns and instruments.
Supports retention-time, molecular-mass and method-performance comparison.
Confirms whether intact peptide remains detectable during the experiment.
Measures peptide loss during storage and sample preparation.
Analytical Characterization
SS-31 is a compact modified tetrapeptide requiring complementary analytical methods.
High-performance liquid chromatography may evaluate chromatographic composition and separate intact peptide from related species.
Liquid chromatography–mass spectrometry may support confirmation of molecular species consistent with the expected intact mass.
Tandem mass spectrometry may provide fragment-ion evidence supporting sequence and terminal structure.
Chiral or specialized methods may be required when confirmation of D-arginine stereochemistry is necessary.
Terminal amidation should be considered during identity analysis.
Counterions, water and residual solvents may contribute to total material mass without representing SS-31 peptide equivalents.
Functional mitochondrial activity cannot be established through chromatographic or mass-spectrometric identity alone.
Total vial mass, SS-31-equivalent content, chromatographic composition, molecular identity, stereochemistry, terminal amidation, counterion form, stability and mitochondrial bioactivity are separate material attributes.
HPLC Analysis of SS-31
Reverse-phase high-performance liquid chromatography may separate SS-31 and related species according to hydrophobic interaction with the stationary phase.
The Dmt and phenylalanine residues contribute aromatic and hydrophobic character.
The D-arginine and lysine residues contribute ionizable basic groups.
Retention behavior may therefore be influenced by mobile-phase pH, ion-pairing reagent, column chemistry, temperature and gradient slope.
Related species may include truncated peptides, terminally modified forms, oxidation products or process-associated compounds.
Detection wavelength influences apparent peak response because SS-31 contains aromatic residues and peptide bonds.
Peak-area percentage does not independently establish total SS-31 content.
Retention time alone does not prove molecular identity and should be supported by mass spectrometry or another orthogonal method.
LC-MS and Molecular Identity
Liquid chromatography–mass spectrometry combines chromatographic separation with mass-to-charge analysis.
SS-31 may produce several ion forms because the molecule contains multiple basic groups.
Singly and multiply protonated ions may be detected depending on mobile phase and source conditions.
Sodium, potassium or other adduct-associated ions may also appear.
Deconvolution may be used to estimate intact neutral molecular mass.
Tandem mass spectrometry may provide sequence-associated fragment ions.
Mass agreement does not independently confirm D- versus L-stereochemistry.
Mass agreement also does not independently establish chromatographic composition, concentration or mitochondrial bioactivity.
Functional Bioactivity Research
Chemical identity and functional mitochondrial activity are distinct properties.
SS-31 bioactivity may be evaluated through cardiolipin-binding, respiration, ATP-production, membrane-potential or oxidative-stress assays.
No single assay represents every proposed SS-31 mechanism.
A cardiolipin-binding result does not independently establish improved cellular respiration.
Improved respiration does not independently establish preservation of mitochondrial ultrastructure.
Functional measurements should be selected according to the research question and supported by appropriate controls.
A validated reference condition may help normalize results across experimental runs.
SS-31 Stability Considerations
SS-31 stability may be influenced by temperature, moisture, light, oxygen, pH, enzymes, concentration and container material.
Potential degradation pathways include peptide-bond hydrolysis, terminal modification, oxidation and proteolytic cleavage.
The Dmt phenolic group and other molecular regions may be evaluated for oxidative change under stressed conditions.
D-arginine may influence susceptibility to selected proteases but does not make the complete peptide universally resistant to degradation.
Lyophilization removes a substantial portion of water and may support stability relative to prolonged solution storage.
Once placed into solution, buffer composition, pH and microbial contamination may become increasingly important.
Appearance alone does not establish intact molecular identity.
Stability should be measured using HPLC, LC-MS or another validated method.
Potential Degradation Pathways
Water-dependent reactions may generate shorter peptide species.
Peptidases may alter the intact tetrapeptide under biological conditions.
Oxygen, light or reactive species may modify susceptible molecular regions.
Alteration of the C-terminal amide would create a distinct molecular species.
Stress conditions may produce structurally related species with altered chromatography.
Peptide may bind to glass, plastic, filters or laboratory tubing.
Proteins, lipids and biological matrices may affect free-peptide recovery.
Related species may overlap with the intact SS-31 chromatographic peak.
Salt content may influence total material mass and analytical behavior.
Contamination may alter peptide integrity and invalidate research measurements.
Laboratory Storage
Lyophilized SS-31 10MG should be maintained in a cool, dry and dark laboratory environment protected from unnecessary heat, moisture and direct light.
Longer-term storage should follow the product label, available lot documentation and validated institutional procedures.
Repeated temperature cycling should be minimized because it may introduce condensation and variable environmental exposure.
When condensation is possible, sealed material should be allowed to equilibrate under controlled laboratory conditions before opening.
Prepared research solutions are generally less stable than dry lyophilized material.
Solution stability depends on pH, buffer composition, oxygen exposure, temperature, concentration, container material and storage duration.
Storage information is provided solely for preservation of laboratory research material and is not a preparation, dosing or administration protocol.
Laboratory Handling
SS-31 10MG should be handled only by trained research personnel using procedures appropriate for synthetic peptide materials.
Researchers should document the lot identifier, preparation date, solvent or buffer, calculated concentration, storage history and handling cycles.
Calibrated balances, pipettes and analytical instruments should be used when quantitative accuracy is required.
Small-volume transfer error, incomplete mixing and surface adsorption may create differences between calculated and recovered concentrations.
Low-binding laboratory materials may be evaluated when adsorption has been demonstrated experimentally.
Filtration methods should be tested for peptide recovery before routine use.
Personal protective equipment, containment procedures and waste disposal should follow institutional requirements and laboratory risk assessment.
SS-31 Compared With Related Research Compounds
SS-31 is a designed cardiolipin-interacting tetrapeptide, while MOTS-c is a 16-residue mitochondrial-derived signaling peptide.
SS-31 is synthetic and cardiolipin-directed, while humanin is a mitochondrial-derived peptide with a distinct sequence and research profile.
SS-31 is a peptide targeting mitochondrial membrane systems, while NAD+ is a nucleotide-derived redox cofactor.
SS-31 is an aromatic-cationic peptide, while MitoQ is a ubiquinone derivative linked to a lipophilic cation.
SS-31 interacts with cardiolipin-associated membranes, while coenzyme Q10 participates directly in respiratory-chain electron transfer.
SS-31 is investigated in mitochondrial membrane biology, while tesamorelin is a GHRH-receptor peptide analogue.
SS-31 vs. MOTS-c Research
SS-31 and MOTS-c are both discussed in mitochondrial research but represent different peptide classes.
SS-31 is a four-residue synthetic aromatic-cationic peptide.
MOTS-c is a 16-residue mitochondrial-derived peptide associated with a short mitochondrial open reading frame.
SS-31 is investigated primarily through cardiolipin, inner-membrane and bioenergetic mechanisms.
MOTS-c is investigated primarily through metabolic signaling, AMPK-associated pathways and nuclear translocation.
SS-31 is not encoded by mitochondrial DNA, and MOTS-c is not a Szeto–Schiller peptide.
Comparative research should use independent pathway-specific endpoints and molar normalization.
SS-31 vs. NAD+ Research
SS-31 and NAD+ are chemically and mechanistically distinct.
SS-31 is a synthetic tetrapeptide investigated in cardiolipin-associated mitochondrial systems.
NAD+ is a nucleotide-derived cofactor participating in redox reactions and enzyme regulation.
Both may influence mitochondrial research endpoints, but shared research context does not establish shared molecular action.
Analytical methods, stability and concentration calculations differ substantially between peptide and nucleotide materials.
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Frequently Asked Questions
What is SS-31 10MG?
SS-31 10MG is a lyophilized laboratory research format containing a nominal 10MG quantity of SS-31.
What is another name for SS-31?
SS-31 is widely known as elamipretide and has also been identified as MTP-131 and Bendavia.
What type of peptide is SS-31?
SS-31 is a synthetic aromatic-cationic, mitochondria-targeted tetrapeptide.
What peptide family does SS-31 belong to?
SS-31 belongs to the Szeto–Schiller peptide family.
What is the SS-31 sequence?
The commonly referenced sequence is D-Arg-Dmt-Lys-Phe-NHâ‚‚.
What does Dmt mean?
Dmt refers to 2,6-dimethyltyrosine, a modified aromatic amino-acid residue.
How many amino acids does SS-31 contain?
SS-31 contains four amino-acid residues.
What is the molecular formula of SS-31?
The commonly referenced free-base molecular formula is C32H49N9O5.
What is the molecular weight of SS-31?
The referenced free-base molecular weight is approximately 639.8 g/mol.
What is the PubChem CID for elamipretide?
The PubChem Compound ID is 11764719.
What is the CAS number for elamipretide?
The commonly referenced CAS number is 736992-21-5.
Does SS-31 contain a disulfide bridge?
No. The four-residue sequence contains no cysteine residues.
Is SS-31 a mitochondrial-derived peptide?
No. SS-31 is a designed synthetic peptide, unlike mitochondrial-derived peptides such as MOTS-c.
What does SS-31 interact with?
SS-31 is primarily investigated for reversible interaction with cardiolipin-containing inner mitochondrial membranes.
What is cardiolipin?
Cardiolipin is a negatively charged phospholipid enriched within the inner mitochondrial membrane.
Why is cardiolipin important?
Cardiolipin contributes to cristae structure, respiratory-protein organization and mitochondrial bioenergetics.
Does SS-31 directly produce ATP?
No. SS-31 is investigated for effects on mitochondrial membrane and respiratory systems that may influence ATP production.
Is SS-31 a conventional antioxidant?
SS-31 is not best described solely as a nonspecific antioxidant. Its research mechanism centers on cardiolipin-associated mitochondrial systems.
Can SS-31 be studied in respiration assays?
Yes. It may be evaluated through basal, ATP-linked, maximal and proton-leak-associated respiration measurements.
Can SS-31 be studied in membrane-potential assays?
Yes. Appropriate controls are required because fluorescent probe behavior depends on several cellular variables.
Can SS-31 be studied in cardiolipin liposomes?
Defined liposome systems may be used to investigate cardiolipin-dependent membrane interaction.
How does SS-31 differ from MOTS-c?
SS-31 is a four-residue cardiolipin-interacting synthetic peptide, while MOTS-c is a 16-residue mitochondrial-derived signaling peptide.
How does SS-31 differ from NAD+?
SS-31 is a peptide, while NAD+ is a nucleotide-derived cellular redox cofactor.
How does SS-31 differ from CoQ10?
SS-31 interacts with cardiolipin-associated membrane systems, while coenzyme Q10 transfers electrons within the respiratory chain.
Why are molar concentrations useful?
Molar concentration controls molecule number when comparing SS-31 with compounds having different molecular weights.
Can HPLC confirm SS-31 identity by itself?
HPLC can evaluate chromatographic behavior, but identity should be supported by LC-MS or another orthogonal method.
Does molecular-mass agreement prove bioactivity?
No. Chemical identity and mitochondrial functional activity are separate properties.
Does the 10MG designation represent a recommended dose?
No. The 10MG designation identifies nominal laboratory research quantity only and does not represent a recommended amount, dosage, schedule or administration instruction.
Is SS-31 10MG intended for human use?
No. It is strictly for controlled laboratory research and is not intended for human or veterinary administration.
Research-Use Notice
SS-31 10MG is supplied exclusively as laboratory research material. It is not a finished pharmaceutical product, prescription medication, generic drug, compounded medication, food, dietary supplement, cosmetic or consumer product. It is not intended for human consumption, self-administration, medical use, veterinary use, household use, diagnostic use, topical application or therapeutic use.
SS-31 is also identified in scientific literature by the research synonym elamipretide. Use of a scientific synonym does not represent this material as an approved medicine, prescription product, generic equivalent, compounded medication or material suitable for clinical or personal use.
References to cardiolipin, mitochondrial membranes, cristae, electron transport, ATP-associated measurements, oxidative stress, muscle models, cardiac models, renal models, neurobiology, retinal models, aging-associated systems or published scientific findings are provided solely to describe areas of laboratory and preclinical investigation.
These references do not constitute medical claims, treatment recommendations or representations regarding the safety or effectiveness of this research material.
Findings from biochemical, cellular, isolated-mitochondrial, tissue or animal models do not establish safety, efficacy, dosing, bioavailability or suitability for administration to humans or animals.
No information on this page should be interpreted as instructions for reconstitution, dosing, administration, injection, self-experimentation, athletic-performance enhancement, anti-aging use, diagnosis, prevention, mitigation or treatment of any disease or condition.
The 10MG designation identifies nominal laboratory research quantity only. It does not represent a recommended amount, dosage, schedule or administration instruction.
This material should be handled only by qualified research personnel in an appropriately controlled laboratory environment. Researchers are responsible for confirming molecular identity, reviewing available lot-specific analytical documentation, selecting suitable analytical methods, determining suitability for their experimental design and complying with all applicable institutional, local, state and federal requirements.
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