Glycyl-L-a-glutamyl-L-prolyl-L-prolyl-L-prolylglycyl-L-lysyl-L-prolyl-L-alanyl-L-a-aspartyl-L-a-aspartyl-L-alanylglycyl-L-leucyl-L-valine acetate (1:1)
[CAS# 216441-37-1]

Identification

• Classification: Biochemical >> Peptide
• Name: Glycyl-L-a-glutamyl-L-prolyl-L-prolyl-L-prolylglycyl-L-lysyl-L-prolyl-L-alanyl-L-a-aspartyl-L-a-aspartyl-L-alanylglycyl-L-leucyl-L-valine acetate (1:1)
• Synonyms: BPC-157 acetate; acetic acid;(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
• Protein Sequence: GEPPPGKPADDAGLV
• Molecular Formula: C₆₄H₁₀₂N₁₆O₂₄
• Molecular Weight: 1479.59
• CAS Registry Number: 216441-37-1
• 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.CC(=O)O

Discovory and Applicatios

Glycyl-L-α-glutamyl-L-prolyl-L-prolyl-L-prolylglycyl-L-lysyl-L-prolyl-L-alanyl-L-α-aspartyl-L-α-aspartyl-L-alanylglycyl-L-leucyl-L-valine acetate (1:1) is a synthetic peptide composed of a defined sequence of naturally occurring amino acids, isolated and characterized as part of broader efforts in peptide chemistry and biochemical research rather than as a naturally occurring biological product. Compounds of this type emerged from the development of solid-phase peptide synthesis in the mid-twentieth century, a methodological breakthrough that enabled chemists to prepare peptides with precise amino acid sequences in reproducible and scalable ways. This technological advance transformed the study of proteins and peptides by allowing systematic investigation of sequence–structure–function relationships using fully synthetic materials.

The discovery of this specific peptide is therefore best understood within the historical context of synthetic peptide research rather than as the isolation of a new natural substance. As peptide synthesis techniques matured, researchers increasingly designed and prepared custom peptides that mirrored fragments of larger proteins or that incorporated repetitive motifs rich in certain amino acids, such as proline or acidic residues. Such sequences were of interest because they allowed the study of conformational preferences, hydrogen bonding patterns, and interactions with enzymes or receptors under controlled conditions. The preparation of peptides containing multiple proline residues, as in this case, was particularly valuable for probing the structural features associated with turns, rigidity, and resistance to enzymatic degradation.

The acetate form of the peptide reflects standard practice in peptide chemistry, where counterions such as acetate are introduced during purification or lyophilization to improve stability and handling. This does not alter the fundamental chemical identity of the peptide backbone or side chains but facilitates its use as a laboratory reagent. The defined stereochemistry, indicated by the L-configuration of each amino acid residue, ensures that the peptide corresponds to the naturally predominant chiral form found in biological systems, which is essential for meaningful biochemical studies.

In terms of application, peptides of this nature are primarily used as research tools. They may serve as model substrates or inhibitors in enzymology, particularly in studies of proteases that recognize specific sequence motifs or secondary structure elements. The presence of multiple acidic residues and prolines makes such peptides suitable for investigating enzyme specificity, binding affinity, and catalytic mechanisms. They are also employed in biophysical experiments, including nuclear magnetic resonance spectroscopy and circular dichroism, to examine peptide conformation and dynamics in solution.

Beyond enzymatic studies, synthetic peptides with well-defined sequences are widely used in immunological and cell biology research. Although there is no evidence that this particular peptide is used as a therapeutic agent or diagnostic marker, peptides of comparable complexity are commonly applied as antigens, epitope mimics, or standards in analytical methods. Their synthetic origin ensures batch-to-batch consistency, which is critical for reproducible experimental outcomes.

Overall, Glycyl-L-α-glutamyl-L-prolyl-L-prolyl-L-prolylglycyl-L-lysyl-L-prolyl-L-alanyl-L-α-aspartyl-L-α-aspartyl-L-alanylglycyl-L-leucyl-L-valine acetate (1:1) represents a product of established peptide synthesis methodologies. Its significance lies not in a singular historical discovery or a specific commercial application, but in its role as a precisely defined molecular tool that supports fundamental research in chemistry, biochemistry, and molecular biology.