| Customization: | Available |
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| CAS No.: | 736992-21-5 |
| Formula: | Chons |
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| Purity | 99%+ | Private customization | 2mg 5mg 10mg 15mg 20mg 30me etc. | |
| Cleanliness | Sterile | Transportation time | 7-15days | |
| Actual peptide content | Exceed the standard | Disguise | Can provide | |
| Test Report | Janoshik Test Report | Resend policy | According to different countries | |
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Mitochondrial dysfunction includes heritable diseases, acquired pathologies, and age-related declines in health. Szeto-Schiller (SS) peptides comprise a class of amphipathic tetrapeptides that have demonstrated efficacy in treating a wide array of mitochondrial disorders, and are believed to target mitochondrial membranes due to their enrichment in the anionic phospholipid cardiolipin (CL). However, little is known regarding how SS peptides interact with or alter the physical properties of lipid bilayers. In this study, we have analyzed the interactions of the lead compound SS-31 (Elamipretide) with model and mitochondrial membranes using biophysical and computational approaches. Our results show that this polybasic peptide partitions into the membrane interfacial region with affinity and binding density that are directly related to surface charge. SS-31 binding does not destabilize lamellar bilayers even at the highest binding concentrations; however, it does cause saturable alterations in lipid packing. Most notably, SS-31 modulates the surface electrostatic properties of model and mitochondrial membranes, which could play a significant role in the mitoprotective properties of this compound. As a proof of concept, we show that SS-31 alters ion distribution at the membrane interface with implications for maintaining mitochondrial membranes subject to divalent cation (calcium) stress. Taken together, these results support a mechanism of action in which SS peptides interact with lipid bilayers and alter the biophysical (primarily electrostatic) properties of mitochondrial membranes as their primary mechanism of action. Understanding this molecular mechanism is key to the development of future compound variants with enhanced efficacy.
Peptides are composed of amino acids linked together by Peptides. The smallest Peptides can consist of three amino acids, such as thyrotropin-releasing hormone (TRH). Most Peptides can be made up of dozens or even hundreds of amino acids. The primary secretion organs for Peptides are the hypothalamus and the pituitary gland; however, Peptides have also been found in other organs, such as the gastrointestinal tract, brain tissue, lungs, and heart. Peptides are a type of endogenous substance that consists of protein chains containing polypeptide compounds. Examples of Peptides include thyrotropin-releasing hormone, Peptides and its analogs, Peptides and its analogs, adrenocorticotropic hormone, gonadotropins, Peptides and its analogs, Peptides-like Peptides, calcitonin, and parathyroid hormone.
2:Metabolic Effects: They increase muscle mass and enhance tendon strength, resulting in stronger muscles and increased power, providing a competitive advantage. This is one reason why they are used as performance enhancers.
3:Anti-Aging Effects: They are frequently used in the field of cosmetics.
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