Research reference library
Reference chemistry and published preclinical literature for the compounds in the AlpineChems catalog. Each entry lists identifiers, characterisation methods, handling requirements, and primary sources. Materials are supplied for laboratory research use only.
BPC-157
BPC-157 is a synthetic pentadecapeptide. Its fifteen residues run Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val, giving a free-peptide formula of C62H98N16O22 and an average mass close to 1419.5 daltons. No cysteine is present, so there is no disulfide bridge to reduce or scramble. Three consecutive prolines occupy positions three through five, and that block together with the acidic pair at Asp10 and Asp11 governs how the chain behaves in solution. The residue tally runs three acidic against one basic, leaving the free peptide with a net negative charge at neutral pH.
GHK-Cu
GHK-Cu is the copper(II) complex of glycyl-L-histidyl-L-lysine, a tripeptide of the sequence Gly-His-Lys. The free peptide has the formula C14H24N6O4 and a mass near 340 daltons. Copper is held by three nitrogen donors: the N-terminal amine, the deprotonated amide nitrogen of the glycyl-histidyl bond, and the imidazole nitrogen of the histidine side chain. The affinity of the tripeptide for the metal is close to that of the amino-terminal copper transport site of serum albumin, which is the comparison drawn in the earliest characterisation work. The side-chain amine of the lysine residue takes no part in coordination and leaves the complex cationic near neutral pH.
MOTS-c
MOTS-c is a peptide of sixteen residues with the sequence MRWQEMGYIFYPRKLR. Its coding region sits inside the 12S ribosomal RNA gene of the mitochondrial genome, on a short open reading frame that overlaps the rRNA itself. Translation is understood to take place in the cytoplasm under the standard genetic code, which is why the published sequence differs from what the mitochondrial code would give for the same stretch of DNA. That detail is not incidental. It underpins the case for a genuine mitochondrial DNA product that acts outside the organelle.
KPV
KPV is a tripeptide of lysine, proline and valine, written Lys-Pro-Val in three-letter code. The free acid has the formula C16H30N4O4 and an average mass near 342.4 daltons. The sequence is not arbitrary. It reproduces residues 11 to 13 of alpha-melanocyte-stimulating hormone, the C-terminal tripeptide of that thirteen-residue melanocortin, which is itself a proteolytic product of proopiomelanocortin.
DSIP
DSIP is a nonapeptide. The sequence runs Trp-Ala-Gly-Gly-Asp-Ala-Ser-Gly-Glu, or WAGGDASGE in single-letter code, and the acronym expands to Delta Sleep-Inducing Peptide. The neutral molecule has the formula C35H48N10O15 and an average mass close to 849 daltons, the figure quoted throughout the older literature. Six of the nine residues are glycine, alanine or serine. What remains is one tryptophan and two acidic side chains, so the chain is small, flexible, strongly hydrophilic and carries no basic residue at all.
Tesamorelin
Tesamorelin is a synthetic analogue of human growth hormone releasing hormone. It reproduces the full 44 residue sequence of hGHRH as the C-terminal amide and carries a trans-3-hexenoyl group anchored on the tyrosine at position one. That acyl cap is the reason the molecule exists. Native GHRH is cleaved at the Tyr1-Ala2 bond by dipeptidyl peptidase IV within minutes of entering plasma, and the hexenoyl modification obstructs the reaction without disturbing the helical region the receptor reads. Reported plasma stability improves by roughly an order of magnitude against the unmodified sequence.
MT-1
MT-1 is a synthetic analogue of alpha-melanocyte-stimulating hormone, the tridecapeptide released by processing of pro-opiomelanocortin. Two substitutions define it. Norleucine replaces the methionine at position 4, which removes the oxidation-labile side chain of the parent sequence. D-phenylalanine replaces the L residue at position 7, inverting the stereocentre at the position that sets the geometry of the His-Phe-Arg-Trp core. Neither change touches the message sequence itself.
MT-2
MT-2 is a conformationally constrained analogue of alpha-melanocyte-stimulating hormone with the structure Ac-Nle4-cyclo[Asp5, D-Phe7, Lys10]-alpha-MSH(4-10)-NH2. Seven residues remain of the thirteen carried by the parent hormone. A lactam bridge joins the side-chain carboxyl of Asp5 to the side-chain amine of Lys10, so the ring closes through side chains and leaves the backbone termini capped as an acetyl group and a primary amide.
5-Amino-1MQ
5-Amino-1MQ is 5-amino-1-methylquinolinium, a small molecule and not a peptide. The scaffold is a quinoline, a benzene ring fused to a pyridine, with the ring nitrogen permanently methylated and a primary amine at position five. The cation has the formula C10H11N2 and carries a fixed positive charge, so the material is supplied as a salt paired with a counterion. PubChem catalogues the free cation as CID 950107.
Glutathione
Glutathione is a tripeptide of glutamate, cysteine and glycine, written gamma-Glu-Cys-Gly. That abbreviation misleads in one respect. The bond joining glutamate to cysteine runs from the glutamate side chain carboxyl rather than the alpha carboxyl, so the molecule is not a peptide in the ribosomal sense and no tRNA route produces it. Two ATP-dependent ligases build it instead. That gamma linkage also puts the internal amide out of reach of most aminopeptidases, which is why the intracellular pool persists at millimolar concentration rather than turning over in minutes.
NAD+
Nicotinamide adenine dinucleotide is two nucleotides joined tail to tail. An adenosine monophosphate and a nicotinamide mononucleotide share a pyrophosphate bridge, so the molecule presents an adenine at one end, a nicotinamide at the other, and two ribose rings in between. The adenine half is largely structural. It supplies the binding determinants that Rossmann-fold enzymes recognise. The chemistry happens at the nicotinamide.
Certificates of Analysis for stocked lots are published on the lab results page.