Skip to content

Study · In vitro (cell-free) · 2026

3 results

BPC-157 and Its Novel Hybrid Analogs as Inhibitors of Acetylcholinesterase.

Jelińska J, Józwiak M, Szeleszczuk Ł, Sikora K, Kamysz W, Kleczkowska P, Gackowski M, Grodner B

International journal of molecular sciences30 May 2026

PMID42278509 (opens in a new tab)PMCIDPMC13257072 (opens in a new tab)DOI10.3390/ijms27114984 (opens in a new tab)PepBankPUB-42278509
Download PDFPubMedAsk about this study
Jump to 3 results

Summary

Acetylcholinesterase (AChE) inhibition remains a key therapeutic strategy in the management of neurodegenerative disorders such as Alzheimer's disease. In this study, the inhibitory potential of the gastric pentadecapeptide BPC-157 and two newly designed hybrid analogs, CIARA-1 and CIARA-2, was investigated for the first time. The hybrid peptides were rationally designed by combining a BPC-157-derived fragment with an arginine-containing C-terminal sequence to enhance interactions with the enzyme's active and peripheral binding sites. Enzyme kinetics were evaluated using a modified Ellman assay, and inhibition parameters were determined through Lineweaver-Burk analysis. All tested compounds exhibited a competitive mechanism of inhibition, as evidenced by increased Michaelis-Menten constant (Km) values with unchanged maximum velocity (Vmax), indicating competition with the substrate at the catalytic site of AChE. Among the tested compounds, CIARA-1 demonstrated the highest inhibitory potency, reflected by the lowest inhibition constant (Ki = 0.24 mM) and IC50 value (2.52 mM), followed by CIARA-2 (Ki = 0.29 mM; IC50 = 2.73 mM) and BPC-157 (Ki = 0.48 mM; IC50 = 2.80 mM). These findings were consistent with molecular modeling predictions, supporting stronger binding interactions for CIARA-1. Despite significantly lower potency compared to clinically used AChE inhibitors, the studied peptides represent a promising scaffold for further optimization. Overall, this work demonstrates that BPC-157 and its hybrid analogs act as reversible competitive AChE inhibitors, with enhanced activity observed for structurally modified derivatives. The results highlight the potential of peptide-based hybrid molecules as multifunctional candidates in the development of novel therapeutics targeting cholinergic dysfunction.
CC BYText from Europe PMC. Highlighted sentences are the source of results.

Results from this study3

3 results from studies that gave the peptide. No result from this study comes from people.

  1. 01LabIn vitro (cell-free)Mechanism

    In an enzyme assay, BPC‑157 inhibited acetylcholinesterase by a competitive mechanism, with increased Km and unchanged Vmax.

    In plain wordsIn lab tests, BPC‑157 blocked an enzyme (acetylcholinesterase) by competing with the enzyme's normal target.

    Peptide
    BPC-157
    Outcome
    Not applicableMechanism of acetylcholinesterase inhibition
    Study

    n: not reported in source

    Acetylcholinesterase enzyme assay (modified Ellman assay)
    Outcome group
    Receptor activity and mechanism · Nervous system and cognition
    Studied dose
    Dose not stated

    Source sentences

    Summary
    All tested compounds exhibited a competitive mechanism of inhibition, as evidenced by increased Michaelis-Menten constant (Km) values with unchanged maximum velocity (Vmax), indicating competition with the substrate at the catalytic site of AChE.
    1 context sentence
    Summary · context
    Enzyme kinetics were evaluated using a modified Ellman assay, and inhibition parameters were determined through Lineweaver-Burk analysis.
  2. 02LabIn vitro (cell-free)Activity measurement

    In an enzyme assay, BPC‑157 inhibited acetylcholinesterase with a Ki of 0.48 mM, weaker than the analog CIARA-1.

    In plain wordsIn lab tests, BPC‑157 blocked an enzyme (acetylcholinesterase) only weakly.

    Peptide
    BPC-157
    Outcome
    Not applicableAcetylcholinesterase inhibition constant (Ki)
    Study

    n: not reported in source

    Acetylcholinesterase enzyme assay (modified Ellman assay)
    Outcome group
    Receptor activity and mechanism · Nervous system and cognition
    Studied dose
    Dose not stated

    Measurements

    Ki
    0.48 mM
    acetylcholinesterase

    Source sentences

    Summary
    and BPC-157 (Ki = 0.48 mM; IC50 = 2.80 mM).
    1 context sentence
    Summary · context
    Enzyme kinetics were evaluated using a modified Ellman assay, and inhibition parameters were determined through Lineweaver-Burk analysis.
  3. 03LabIn vitro (cell-free)Activity measurement

    In an enzyme assay, BPC‑157 inhibited acetylcholinesterase with an IC50 of 2.80 mM.

    In plain wordsIn lab tests, BPC‑157 needed a high concentration to block an enzyme (acetylcholinesterase).

    Peptide
    BPC-157
    Outcome
    Not applicableAcetylcholinesterase inhibition IC50
    Study

    n: not reported in source

    Acetylcholinesterase enzyme assay (modified Ellman assay)
    Outcome group
    Receptor activity and mechanism · Nervous system and cognition
    Studied dose
    Dose not stated

    Measurements

    IC50
    2.8 mM
    acetylcholinesterase

    Source sentences

    Summary
    and BPC-157 (Ki = 0.48 mM; IC50 = 2.80 mM).
    1 context sentence
    Summary · context
    Enzyme kinetics were evaluated using a modified Ellman assay, and inhibition parameters were determined through Lineweaver-Burk analysis.

AI wrote and checked these results. AI can make mistakes, so check important results against the source.

Version history

PepBank keeps every version of the data on this study. Status changes from Retraction Watch, Europe PMC and Crossref are listed with their source.

  1. Version 3Current

    10 Oct 2026, 08:19 UTC

    Study results updated

  2. Version 2

    9 Oct 2026, 03:03 UTC

    Study data updated · source update from Europe PMC

  3. Version 1

    9 Oct 2026, 02:56 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

PepBank is a research reference. Talk to a doctor before you use any peptide.