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| Classification | Biochemical >> Peptide |
|---|---|
| Name | Glycyl-L-alpha-glutamyl-L-prolyl-L-prolyl-L-prolylglycyl-L-lysyl-L-prolyl-L-alanyl-L-alpha-aspartyl-L-alpha-aspartyl-L-alanylglycyl-L-leucyl-L-valine |
| Synonyms | BPC 157 trifluoroacetate salt; (4S)-4-[(2-aminoacetyl)amino]-5-[(2S)-2-[(2S)-2-[(2S)-2-[[2-[[(2S)-6-amino-1-[(2S)-2-[[(2S)-1-[[(2S)-3-carboxy-1-[[(2S)-3-carboxy-1-[[(2S)-1-[[2-[[(2S)-1-[[(1S)-1-carboxy-2-methylpropyl]amino]-4-methyl-1-oxopentan-2-yl]amino]-2-oxoethyl]amino]-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]carbamoyl]pyrrolidin-1-yl]-1-oxohexan-2-yl]amino]-2-oxoethyl]carbamoyl]pyrrolidine-1-carbonyl]pyrrolidine-1-carbonyl]pyrrolidin-1-yl]-5-oxopentanoic acid |
| Molecular Structure | ![]() |
| Protein Sequence | 1-15 GEPPPGKPAD DAGLV [15-E-OH;] |
| Molecular Formula | C62H98N16O22 |
| Molecular Weight | 1419.54 |
| CAS Registry Number | 137525-51-0 |
| SMILES | C[C@@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C(C)C)C(=O)O)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CCCCN)NC(=O)CNC(=O)[C@@H]2CCCN2C(=O)[C@@H]3CCCN3C(=O)[C@@H]4CCCN4C(=O)[C@H](CCC(=O)O)NC(=O)CN |
| Solubility | Freely soluble (990 g/L) (25 ºC), Calc.* |
|---|---|
| Density | 1.366±0.06 g/cm3 (20 ºC 760 Torr), Calc.* |
| Index of Refraction | 1.576, Calc.* |
| Boiling Point | 1802.9±65.0 ºC (760 mmHg), Calc.* |
| Flash Point | 1044.2±34.3 ºC, Calc.* |
| * | Calculated using Advanced Chemistry Development (ACD/Labs) Software. |
| SDS | Available |
|---|---|
|
Glycyl-L-alpha-glutamyl-L-prolyl-L-prolyl-L-prolylglycyl-L-lysyl-L-prolyl-L-alanyl-L-alpha-aspartyl-L-alpha-aspartyl-L-alanylglycyl-L-leucyl-L-valine is a complex peptide composed of multiple amino acid residues. This intricate structure highlights the growing interest in peptide research, particularly in the realms of biochemistry and pharmacology. While the compound may not be widely recognized, its composition and potential applications make it a subject of exploration in various scientific fields. The discovery of this peptide sequence stems from advances in peptide synthesis and the understanding of peptide functions in biological systems. Researchers have long studied peptides for their roles in cell signaling, enzyme regulation, and as potential therapeutics. The specific sequence of this peptide suggests that it may exhibit unique biological properties that could be harnessed for medicinal purposes. Peptides, including this particular sequence, have garnered attention in drug discovery and development due to their high specificity and affinity for biological targets. Their structural complexity allows them to interact with a variety of receptors and enzymes, making them suitable candidates for therapeutic applications. This peptide, with its rich composition of proline and other amino acids, may influence protein folding, stability, and interactions, potentially providing insights into the design of novel therapeutic agents. In addition to their therapeutic potential, peptides are increasingly used in research as tools for probing biological processes. This specific peptide could serve as a model compound for studying the effects of peptide structure on biological activity, offering insights into how modifications can enhance or diminish function. By exploring its interactions with various cellular targets, scientists can better understand the mechanisms underlying peptide activity and apply this knowledge to develop targeted therapies. Furthermore, peptides like this one are being investigated for their roles in drug delivery systems. The ability of certain peptides to facilitate cellular uptake and transport makes them attractive candidates for delivering therapeutic agents directly to target cells or tissues. Researchers are exploring how this peptide can be utilized to enhance the bioavailability of drugs, particularly in challenging therapeutic areas such as cancer treatment or neurological disorders. Despite its potential, the application of this specific peptide in clinical settings remains to be fully explored. Ongoing research is needed to investigate its stability, efficacy, and safety profile. As peptide synthesis technologies continue to advance, the opportunities for studying and utilizing complex peptide structures like this one will expand, paving the way for novel therapeutic strategies. In summary, Glycyl-L-alpha-glutamyl-L-prolyl-L-prolyl-L-prolylglycyl-L-lysyl-L-prolyl-L-alanyl-L-alpha-aspartyl-L-alpha-aspartyl-L-alanylglycyl-L-leucyl-L-valine is a complex peptide that represents the ongoing exploration of peptide-based therapeutics and research tools. Its discovery and potential applications underscore the significance of peptides in advancing our understanding of biological processes and developing innovative therapeutic solutions. References 1993. A new gastric juice peptide, BPC. An overview of the stomach-stress-organoprotection hypothesis and beneficial effects of BPC. Journal of Physiology, Paris, 87(5). DOI: 10.1016/0928-4257(93)90038-u 2019. Stable gastric pentadecapeptide BPC 157 in the therapy of the rats with bile duct ligation. European Journal of Pharmacology, 847. DOI: 10.1016/j.ejphar.2019.01.030 2023. Stable Isotope Labeling-Based Nontargeted Strategy for Characterization of the In Vitro Metabolic Profile of a Novel Doping BPC-157 in Doping Control by UHPLC-HRMS. Molecules, 28(21). DOI: 10.3390/molecules28217345 |