The short version of amino acid sequence fits in a sentence. The long version — which is the one that helps — is below.
This page was last updated on 2026-08-01 and is reviewed periodically as new material appears.
BPC-157 is a synthetic peptide built from fifteen amino acid residues. Its sequence comes from a larger protein fragment that researchers isolated from human gastric juice and described as a body protection compound. The fragment contains glycine, glutamic acid, five prolines, lysine, alanine, two aspartic acids, leucine, and valine. The number 157 in the name refers to the position of the stretch within the parent protein. Material used in laboratories is manufactured rather than extracted from stomach fluid.
The molecule carries 15 residues, a molar mass near 1419.5 g/mol, and the formula C62H98N16O22. Its structure features a proline-rich central region, a pair of adjacent aspartic acid residues, and no cysteine. The absence of cysteine means no disulfide bonds can form, which simplifies refolding and reconstitution. Suppliers usually ship the material as a freeze-dried powder that appears white to off-white. It dissolves readily in water and in saline solutions.
Supplied material is typically a lyophilized white to off-white powder. The peptide is freely soluble in water and in common aqueous buffers, which allows it to be handled as a stock solution. Because the sequence contains no cysteine, disulfide cross-linking is not a route of degradation. The absence of aromatic residues means ultraviolet absorbance at 280 nm is minimal, so quantification usually relies on peptide bond absorbance near 214 nm or on amino acid analysis.
Common synonyms in catalogs include pentadecapeptide BPC 157, BPC157, and the full sequence name. A CAS registry number in the 137525-51-0 range is frequently listed, though the assignment should be verified against the supplier certificate of analysis. The name itself is not a pharmacopoeial designation, and there is no standardized international nonproprietary name. Distinguishing genuine material from related fragments generally requires mass spectrometry, since several truncated sequences share similar chromatographic behavior.
| Property | Value | Notes |
|---|---|---|
| Molar mass | Approximately 1419.5 g/mol | Calculated from the reported 15-residue sequence |
| Molecular formula | C62H98N16O22 | Based on the same sequence |
| Appearance | White to off-white powder | Typical of a lyophilized preparation |
| Solubility class | Freely soluble in water | Also dissolves in saline solutions |
| Typical storage temperature | Minus 20 degrees Celsius, dry | Refrigeration advised after reconstitution |
BPC-157 is a synthetic fifteen-amino-acid peptide whose sequence is GEPPPGKPADDAGLV. Its name derives from the phrase body protection compound, a term applied to a protein fraction originally detected in human gastric juice. The short peptide is not that full protein; it corresponds to a stable fragment of the larger molecule. Researchers frequently describe it as a pentadecapeptide because it contains exactly fifteen residues. Its neutral molecular mass is approximately 1419 daltons.
The sequence places several glycine and proline residues near the middle, which may influence how the chain folds in solution. The peptide is linear rather than cyclic, and it carries no disulfide bridges. Commercial material is commonly supplied as the acetate salt, although the free base and other counterion forms also appear. Because the term BPC-157 refers to a specific sequence, samples with slight sequence variants are chemically different substances. Published work generally treats the fifteen-residue sequence as the defining structure.
Physical descriptions in supplier documents and papers usually list the compound as a white to off-white powder. It dissolves readily in water and in common aqueous buffers, and solutions are often prepared fresh before an experiment. Molecular mass near 1419 daltons helps verify identity during mass spectrometry. The powder is somewhat hygroscopic, so moisture exposure can alter the measured mass of a sample. Purity is typically reported as a percentage from chromatographic analysis.
BPC-157 is a synthetic pentadecapeptide, meaning it consists of fifteen amino acids joined in a single chain. Its sequence is Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val, a fragment corresponding to part of a larger protein found in human gastric juice. The peptide was first described in the 1990s by researchers in Zagreb who were studying gastric protective factors. It is not a naturally circulating hormone; it is a laboratory-made fragment derived from a stomach protein. The name is an abbreviation of body protection compound, with the number referring to the fragment's position in the source protein.
Most published work on BPC-157 comes from animal experiments rather than controlled human trials. Rodent models have examined its effects on gastrointestinal lesions, tendon and ligament injury, and blood vessel formation. These studies are often small and originate from a limited number of research groups, which affects how broadly the findings can be generalized. No large randomized human trial has been reported in the peer-reviewed literature. Discussion of the compound therefore rests largely on preclinical data, and questions about its effects in people remain open rather than settled.
Several mechanisms have been proposed to explain the activity observed in animal models. The most frequently cited involve signaling through vascular endothelial growth factor receptor 2 and modulation of the nitric oxide system. Researchers have also described interactions with protective pathways in the gut lining. These proposed mechanisms appear in the literature as hypotheses supported by preclinical observations, not as confirmed pathways in humans. The precise way the peptide produces its reported effects, and whether those effects carry across species, remain areas of active and unresolved investigation.
== Relationship to similar concepts == Gene sharing is related to, but distinct from, several concepts in genetics, evolution, and molecular biology. Gene sharing entails multiple effects from the same gene, but unlike pleiotropy, it necessarily involves separate functions at the molecular level. A gene could exhibit pleiotropy when single enzyme function affects multiple phenotypic traits; mutations of a shared gene could potentially affect only a single trait. Gene duplication followed by differential mutation is another phenomenon thought to be a key element in the evolution of protein function, but in gene sharing, there is no divergence of gene sequence when proteins take on new functions; the single polypeptide takes on new roles while retaining old ones. Alternative splicing can result in the production of multiple polypeptides (with multiple functions) from a single gene, but by definition, gene sharing involves multiple functions of a single polypeptide.
counterion The ion that is the counterpart to an oppositely charged ion in a dissociated ionic species; the cation that pairs with a given anion, or vice versa. For example, Na+ is the counterion to Cl−, and vice versa, in solutions of sodium chloride (NaCl).
=== Biosensors === Aminopeptidases have been utilized in creating biosensors for detecting specific amino acids or peptides. These biosensors generate a measurable signal in the presence of the target analyte, leveraging the catalytic activity of aminopeptidases.
(Some contemporary authors question even this single exception, preferring to consistently follow the valence configurations and place helium over beryllium.) There are eight columns in this periodic table fragment, corresponding to at most eight outer-shell electrons. A period begins when a new shell starts filling. Finally, the colouring illustrates the blocks: the elements in the s-block (coloured red) are filling s orbitals, while those in the p-block (coloured yellow) are filling p orbitals.
Sources: en.wikipedia.org
In Mexico, for example, the illicit trafficking of cannabis is thought to constitute the majority of many of the cartels' earnings, and the main way in which the cartels finance many other illegal activities; including the purchase of other illegal drugs for trafficking, and for acquiring weapons that are ultimately used to commit murders (causing a burgeoning in the homicide rates of many areas of the world, but particularly Latin America). Some studies show that the increased legalization of cannabis in the United States (beginning in 2012 with Washington Initiative 502 and Colorado Amendment 64) has led Mexican cartels to smuggle less cannabis in exchange for more heroin.
A linear series of three quadrupoles is known as a triple quadrupole mass spectrometer. The first (Q1) and third (Q3) quadrupoles act as mass filters, and the middle (q2) quadrupole is employed as a collision cell. This collision cell is an RF-only quadrupole (non-mass filtering) using Ar, He, or N2 gas (~10−3 Torr, ~30 eV) for collision induced dissociation of selected parent ion(s) from Q1. Subsequent fragments are passed through to Q3 where they may be filtered or fully scanned. This process allows for the study of fragments that are useful in structural elucidation by tandem mass spectrometry. For example, the Q1 may be set to 'filter' for a drug ion of known mass, which is fragmented in q2. The third quadrupole (Q3) can then be set to scan the entire m/z range, giving information on the intensities of the fragments. Thus, the structure of the original ion can be deduced. The arrangement of three quadrupoles was first developed by Jim Morrison of La Trobe University in Australia for the purpose of studying the photodissociation of gas-phase ions. The first triple-quadrupole mass spectrometer was developed at Michigan State University by Christie Enke and graduate student Richard Yost in the late 1970s. Quadrupoles can be used in hybrid mass spectrometers. For example, a sector instrument can be combined with a collision quadrupole and quadrupole mass analyzer to form a hybrid instrument.
Traditionally, sun drying has been used for some products such as tomatoes, mushrooms, and beans, spreading the produce on racks and turning the crop at intervals. This method suffers from several disadvantages including lack of control over drying rates, spoilage when drying is slow, contamination by dirt, wetting by rain, and attack by rodents, birds, and insects. These disadvantages can be alleviated by using solar powered driers. The dried produce must be prevented from reabsorbing moisture during storage. High levels of both sugar and salt can preserve food by preventing micro-organisms from growing. Green beans can be salted by layering the pods with salt, but this method of preservation is unsuited to most vegetables. Marrows, beetroot, carrot, and some other vegetables can be boiled with sugar to create jams. Vinegar is widely used in food preservation; a sufficient concentration of acetic acid prevents the development of destructive micro-organisms, a fact made use of in the preparation of pickles, chutneys and relishes. Fermentation is another method of preserving vegetables for later use. Sauerkraut is made from chopped cabbage and relies on lactic acid bacteria which produce compounds that are inhibitory to the growth of other micro-organisms.
Sources: en.wikipedia.org
It does not occur in the form that is supplied commercially. Its sequence matches a fragment of a larger gastric protein, and the research material is produced synthetically in a laboratory. The fragment described in the early literature is generally the same synthetic pentadecapeptide.
It marks the position of the sequence inside the original protein. The label traces back to early work fractionating gastric juice and describing a body protection compound. The figure does not refer to molecular weight or to the count of amino acids.
No. The sequence has no cysteine residues, so disulfide bridges cannot form. That feature makes it easier to handle than many small proteins that depend on multiple cysteines for structure.
It is a synthetic peptide built from fifteen amino acids, with a mass of roughly 1419 daltons. The sequence is reported to match a fragment of a protein present in human gastric juice. It is not a naturally circulating hormone.