If you have been reading about research chemical and want a single page that covers the useful parts, this is it: definitions, context, how it is studied, and the questions that come up repeatedly.
Updated 2026-05-10. Numbers and descriptions here follow the published literature rather than marketing material.
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.
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 findings come from rodent experiments using induced injury or surgical models. Human reports remain scarce and are largely observational, which limits how much can be stated with confidence. Questions about absorption, distribution, metabolism, and clearance in people are still open. Dose translation between species is likewise unresolved. Researchers tend to read the animal literature as a starting point rather than a settled account.
BPC-157 is a synthetic peptide composed of fifteen amino acids. Its sequence corresponds to part of a protein found in human gastric juice, which is the origin of the "body protection compound" label. In laboratory work the material is treated as a defined research chemical rather than a finished product. Published research has centered on animal models, and the peptide is not an approved medicine in most countries.
| Property | Value | Notes |
|---|---|---|
| Molecular class | Synthetic pentadecapeptide | Composed of fifteen amino acid residues |
| Amino acid sequence | Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val | Single-letter form GEPPPGKPADDAGLV |
| Original source | Fragment of a protein in human gastric juice | First characterized in the 1990s |
| Number in name | 157 | Refers to the fragment's position in the source protein |
| Human trial evidence | Limited | Preclinical rodent data predominate |
Doses in the literature are usually expressed in micrograms or nanograms per kilogram of body weight. Investigators have administered the peptide by several routes, including injection and oral delivery, depending on the question asked. Route and dose vary widely across studies, which complicates direct comparison of results. Many papers report effects at low doses, but the absence of a standardized protocol limits generalization. Reporting practice differs between research groups.
Some properties, such as the peptide's sequence and molecular mass, are firmly established. Other claims, particularly about mechanism and clinical benefit, remain open questions. Proposed mechanisms include effects on nitric oxide signaling and on cell migration, but these are hypotheses supported by limited evidence. Reviewers often note that the field lacks large controlled human trials. Positive animal findings are best treated as signals for further study rather than as settled conclusions.
Most published studies examine BPC-157 in animal models rather than in humans. Common subjects include rats and mice, and researchers often use models of tissue injury, surgery, or induced inflammation. Reported endpoints include healing rates, blood vessel formation, and markers of tissue repair. These designs provide controlled comparisons, but findings in animals do not automatically transfer to people. Human clinical data remain limited and are frequently described as preliminary.
Material of this kind is sold for laboratory research, and labels typically state that it is not intended for human or veterinary use. In many countries it is not an approved medicine, and sports antidoping rules place it among prohibited non-approved substances. Buyers commonly review a certificate of analysis, an independent test report, and the declared storage conditions. Batch-to-batch variation in purity and in counterion content is possible, and how much that variation affects experimental outcomes remains an open question.
Lyophilized peptide is normally kept at minus twenty degrees Celsius or colder, away from light and moisture. Powder held under those conditions is widely treated as stable for long periods, although published stability studies for this exact sequence are sparse and often come from suppliers rather than independent laboratories. Once dissolved, solutions are generally handled cold and used within a short window, because peptide bonds can hydrolyze over time. Repeated freeze-thaw cycles are usually avoided to limit losses, and exact shelf-life figures depend on the buffer and the concentration involved.
Published storage guidance follows general peptide practice rather than product-specific studies. The dry powder is typically kept at minus 20 degrees Celsius, away from light and moisture. Once reconstituted, solutions are generally refrigerated and used over days to weeks, because the aqueous environment slowly promotes hydrolysis and oxidation. Long-term data on degradation rates or breakdown products are sparse. Stated shelf lives from different producers vary widely, reflecting the absence of a shared reference standard.
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.
Most published work on BPC-157 consists of preclinical studies, including rodent models of tissue injury, gastrointestinal lesions, and vascular or tendon damage, together with in vitro cell assays. Reviews frequently note that the mechanisms proposed in these papers remain incompletely characterised and that findings have not been confirmed in large randomised human trials. The compound is widely sold as a research chemical rather than a licensed medicine, and labels commonly carry a statement that it is not for human use. Whether any of the reported animal effects translate to humans is an open question rather than an established result.
Terminology in the literature is not fully standardised. Papers and product listings use BPC-157, BPC 157, and the longer phrase stable gastric pentadecapeptide BPC 157 interchangeably, and synonyms such as bepecin or PL 14736 appear in older or company-linked publications. Purity claims and reported masses can also differ between sources because peptide preparations may include counterions, residual solvents, or bound water. This variability complicates direct comparison of results across studies and makes the exact identity and grade of a given sample worth verifying. Discussions of the compound should therefore specify the source, salt form, and stated purity where those are known.
BPC-157 is a synthetic peptide composed of fifteen amino acid residues, with the sequence Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val. Its name derives from body protection compound, a term used for a protein fraction identified in human gastric juice. Researchers in Zagreb first reported the pentadecapeptide in the early 1990s and described it as a stable fragment of that larger protein. The compound is also catalogued as PL 14736 and, in some commercial contexts, as bepecin. Its molecular formula is C62H98N16O22 and its monoisotopic mass is approximately 1419 daltons.
=== Unerwünschte Wirkungen === Zu den häufig auftretenden Nebenwirkungen zählen Schwindel, Kopfschmerzen, Atemwegsinfektionen, Hypotonie (zu niedriger Blutdruck), Nierenfunktionsstörungen sowie erhöhte Kaliumwerte im Blut.
Candesartan besitzt in seiner chemischen Struktur einen Tetrazol-Ring und gehört damit zu jenen Sartanen, die potentiell durch Nitrosamin-Verunreinigungen betroffen sein können („Valsartan-Skandal“). Anfang Juli 2018 wurden Chargen gewisser Sartane, darunter neben Valsartan und anderen auch Candesartan, zurückgerufen, weil der Verdacht bestand, dass sie durch krebserregende Dialkylnitrosamine, u. a N-Nitrosodimethylamin (NDMA), verunreinigt waren. Die Rückrufaktion löste international ein erhebliches Medienecho aus und führte zum Teil zum ersatzlosen Absetzen der Medikamente.
== Umweltrelevanz == Wie mehrere andere Sartane zersetzt sich Candesartan unter Bildung der sehr persistenten und sehr mobilen Valsartansäure. Sie stellt ein Problem für die Trinkwassergewinnung dar, da sie sich bei der konventionellen Abwasserbehandlung nicht zersetzt und sich so in Gewässern und im Grundwasser bis zum Gesundheitlichen Orientierungswert (GOW im Trinkwasser = 0,3 μg/L) anreichert. Selbst bei einer Behandlung mittels der sogenannten vierten Reinigungsstufe werden bei Ozonverfahren nur bis zu 39 und mittels Aktivkohle bis zu 43 % eliminiert. Candesartan ist eine der Leitchemikalien der Schweizer Kontrollliste für die Einschätzung der Klärleistung in der vierten Reinigungsstufe.
== Literatur == Europäisches Arzneibuch. 10. Ausgabe. Grundwerk 2020, Band 3. Deutscher Apotheker Verlag, S. 3111. Holger Projahn, Jörg Peters: Candesartancilexetil. In: Wolfgang Blaschek et al. (Hrsg.): Hagers Enzyklopädie der Arzneistoffe und Drogen. 6. Auflage. Band 3. S. 655–660, Wissenschaftliche Verlagsgesellschaft, Stuttgart 2007, ISBN 978-3-8047-2384-9. Axel Kleemann, Jürgen Engel, Bernhard Kutscher, Dietmar Reichert: Pharmaceutical Substances. 5. Auflage. Thieme, Stuttgart / New York 2009, ISBN 978-3-13-558405-8, S. 212–214. Janos Fischer, C. Robin Ganellin (Hrsg.): Analogue-Based Drug Discovery. Wiley-VCH, Weinheim 2006, ISBN 3-527-31257-9, S. 471.
Sources: de.wikipedia.org
It is a chain of fifteen amino acids, referred to as a pentadecapeptide. The sequence is Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val. It corresponds to a fragment of a protein found in human gastric juice.
It is neither a naturally circulating hormone nor an approved medicine in most countries. It is a synthetic peptide fragment used chiefly as a laboratory research material. Its regulatory status varies by jurisdiction, and it is not authorized as a therapeutic product in the United States or the European Union.
Published human evidence is very limited. Most findings come from rodent studies conducted by a small number of groups. As a result, statements about its effects in humans are generally described as uncertain rather than established.
The peptide is synthetic, but its sequence matches a segment of a protein present in human gastric juice. It does not occur as a free fifteen-residue peptide in the body.