Top 7 Healing & Recovery Peptides

BPC-157 (Body Protection Compound-157) is a synthetic peptide consisting of 15 amino acids. It is derived from a partial sequence of a protective protein found in human gastric juice. BPC-157 has become one of the most extensively studied peptides in preclinical research, with over 100 published studies examining its effects in various animal models.

TB-500 is a synthetic analog of Thymosin Beta-4, a naturally occurring 43-amino acid peptide present in virtually all human and animal cells. TB-500 represents the active region of the parent protein and is widely used in research settings to study cell migration, blood vessel formation, and tissue repair mechanisms.

GHK-Cu (copper peptide) is a naturally occurring tripeptide with a strong affinity for copper(II) ions. First identified in human plasma by Dr. Loren Pickart in 1973, GHK-Cu concentration declines with age. It has become one of the most studied peptides in dermatological and aging research, with applications spanning skin biology, wound healing, and gene expression modulation.

KPV is a naturally occurring tripeptide derived from the C-terminal end of alpha-melanocyte-stimulating hormone (alpha-MSH). Despite its extremely small size — just three amino acids — KPV retains significant biological activity related to immune modulation and inflammatory pathway regulation. Its simplicity and stability make it an attractive research tool.

Thymosin Alpha-1 (Ta1) is a 28-amino acid peptide originally isolated from thymic tissue by Allan Goldstein at the George Washington University in the 1970s. It is one of the most extensively studied immunomodulatory peptides, with a substantial body of research spanning several decades. A synthetic version (thymalfasin) has been approved as a pharmaceutical product in over 35 countries for various indications.

SS-31 (also known as Elamipretide or Bendavia) is a synthetic tetrapeptide developed by Dr. Hazel Szeto at Weill Cornell Medical College. It is a mitochondria-targeted antioxidant that selectively concentrates in the inner mitochondrial membrane, specifically binding to cardiolipin — a phospholipid critical for mitochondrial electron transport chain function.

MOTS-c (Mitochondrial Open Reading Frame of the Twelve S rRNA type-c) is a mitochondria-derived peptide discovered by Dr. Changhan Lee at the USC Leonard Davis School of Gerontology in 2015. As one of several recently identified mitochondrial-derived peptides (MDPs), MOTS-c is encoded in the mitochondrial genome rather than the nuclear genome, representing a novel class of signaling molecules.