KPV is the C-terminal peptide stretch of alpha-melanocyte-stimulating hormone (alpha-MSH). The peptide consists of the last three amino acids of the alpha-MSH hormone. It has been explored for its potential anti-inflammatory properties at the cellular level. Comprising the amino acids L-Lys-L-Pro-L-Val, KPV represents the minimal sequence that may mitigate inflammation in experimental models. However, the precise mechanisms of its action still need to be further studied in order to be more fully understood.

This peptide’s various mechanisms may potentially differentiate from that of alpha-MSH, which researchers believe interacts with the melanocortin-1 receptors by theoretically activating the cAMP pathway. Instead, studies suggest a rapid and acute increase in intracellular calcium when KPV is introduced alongside N6-(L-2-phenyl isopropyl) adenosine (PIA), an adenosine agonist that inhibits the cAMP pathway.

Further data-gathering investigations using cells transfected with melanocortin-1 receptors have indicated that KPV may, in theory, elevate intracellular calcium levels. This may imply an additional type of interaction with this receptor. This calcium signaling is thought to contribute to the inhibition of the activation of nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB), a transcription factor involved in inflammatory responses. By potentially inhibiting NF-κB activation, KPV might modulate inflammatory processes within cells.

Specifications

Molecular Formula: C₁₄H₂₂N₄O₉

Molecular Weight: 390.34 g/mol

Sequence: Ala-Glu-Asp-Gly

Other Known Titles: Epitalon, Epithalone, Epithalamin

N-Acetyl Selank is an acetylated form of the Selank peptide. The acetylation of the peptide into N-Acetyl Selank appears to improve its stability. Selank is a synthetic analogue of the natural tetrapeptide Tuftsin. Tuftsin is an immunomodulatory peptide, and N-Acetyl Selank appears to share many of its potential functions. In addition, N-acetyl Selank also appears to exhibit an impact on neurotransmitters, brain signaling, and neuroplasticity.

Oxytocin is a small peptide comprising only nine amino acids, naturally produced in the hypothalamus and secreted by the posterior pituitary gland cells. It has also been isolated from placenta, ovaries, testes, adrenal glands, thymus, retina, and pancreas tissues. The active hormone is obtained by proteolytic cleavage of a larger precursor protein. It is no longer considered merely a neurohypophyseal hormone as its actions are considered to be far-reaching and include interaction with additional peptides. Oxytocin appears to be a protein with two independent natural functions. First, it appears to act as a neuropeptide produced by the hypothalamus to regulate bonding, reproduction, and birth. Oxytocin appears to be bloodborne and secreted by the placenta of pregnant animals to influence birth, milk production, and bonding with their young. Small amounts of the protein produced from testes may promote mating behavior and pair bonding.

Melanotan 1 (MT-1) is a synthetic equivalent of alpha-melanocyte-stimulating hormone (alpha-MSH). The peptide has been exhaustively researched through observation of research models displaying signs of erythropoietic protoporphyria to reduce potential phototoxicity or UV-related damage.^[1] It has been suggested that the peptide may have the potential to influence diverse physiological processes like feeding patterns, central nervous system operations, blood pressure, and more.

PT-141, also known as Bremelanotide, was derived from a synthetic melanocortin analog known as Melanotan 2 (MT-2). A melanocortin analog, such as PT-141 and MT-2, is considered to be any synthetic compound designed to mimic or influence the functions of natural melanocortin peptides. These peptides, such as the alpha-melanocyte stimulating hormone (α-MSH), may be involved in a range of physiological processes including appetite regulation, energy homeostasis, immune responses, and skin cell pigmentation. PT-141 is a melanocortin analog that was developed to interact with Melanocortin-4 Receptor (MC-4R). It has been studied for a variety of potential characteristics and bioactivities through its interaction with this receptor. Apart from MC-4R, there are other melanocortin receptors like MC-1R, MC-2R, MC-3R, and MC-5R, each associated with different potential functions. For instance, MC-1R may be primarily involved in skin cell and hair follicle pigmentation, MC-2R appears to play a crucial role in the adrenal axis and stress response, MC-3R is implicated in the regulation of energy homeostasis, and MC-5R has been linked to exocrine function and thus impacts processes such as sweating and sebum production.

GHK-Cu (Copper Tripeptide) is a tripeptide that scientists assert is naturally present in blood plasma. It has a sequence of Gly-His-Lys (glycine, histidine, and lysine,) which readily binds with copper to form the copper tripeptide. Scientific studies carried out in different research laboratories worldwide have explored its various biological roles. GHK-Cu exhibits some potential to influence various biological pathways, including an apparent induction of tissue repair, attraction of immune cells, antioxidant and anti-inflammatory characteristics, activation of collagen and glycosaminoglycan synthesis in skin fibroblasts, regulation of extracellular matrix components like decorin, and possible promotion of blood vessel growth. Recent studies indicate its potential role in stem cell biology and anti-tumor research as well.

ACE-031 is a soluble protein comprising the type IIB activin receptor (ACVR2B) and the immunoglobulin G1-Fc (IgG1-Fc), and has been studied for its potential in binding and inactivating myostatin, a protein that hampers muscle cell growth. It has been examined during the course of various research studies involved in muscle-wasting disorders and neuromuscular conditions such as Duchenne Muscular Dystrophy (DMD), as well as certain cancers such as those of the prostate or colorectal regions and lipid storage and bone metabolism.