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Study · Not a test of the peptide alone · 2023

2 results

The role of ETFS amino acids on the stability and inhibition of p53-MDM2 complex of anticancer p53-derivatives peptides: Density functional theory and molecular docking studies.

Soriano-Correa C, Vichi-Ramírez MM, Herrera-Valencia EE, Barrientos-Salcedo C

Journal of molecular graphics & modelling13 Apr 2023Cited by 7 (Europe PMC)

PMID37086514 (opens in a new tab)DOI10.1016/j.jmgm.2023.108472 (opens in a new tab)PepBankPUB-37086514
Publisher pagePubMedAsk about this study
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Summary

The text of this summary is not shown here, because the article license does not allow reuse. Read it at the source (opens in a new tab)

Text rights: Publisher copyright. Results still quote short attributed sentences.

Results from this study2

No result from this study comes from a test of the peptide.

Studies that did not test the peptide alone2

In this study, PNC-27 was a lab tool or a carrier, part of a mix, or the subject of a lab method. These results are not evidence about taking PNC-27.

  1. 01Computer modelNot a test of PNC-27 aloneIn silicoMechanism

    In computational models, backbone hydrogen bonds stabilized PNC‑27 alpha-helices more than side-chain hydrogen bonds.

    In plain wordsIn lab computer models, backbone hydrogen bonds stabilized PNC‑27 helices more than side-chain hydrogen bonds.

    Peptide
    PNC-27
    Outcome
    IncreaseAlpha-helix stabilization
    Study

    n: not reported in source

    DFT and molecular docking
    Comparator
    side-chain hydrogen bonds
    Outcome group
    Receptor activity and mechanism · Cancer

    Source sentences

    Summary
    The hydrogen bonds formed by the backbone atoms for PNC-27, PNC-27-B and PNC-28 stabilize the α-helices more than hydrogen bonds formed by the side chains atoms.
    1 context sentence
    Summary · context
    by means of chemical descriptors at the DFT-BHandHLYP level in an aqueous solution, and its intermolecular interactions through molecular docking studies.

    In this study, PNC-27 was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking PNC-27.

  2. 02Computer modelNot a test of PNC-27 aloneIn silicoMechanism

    In molecular docking, PNC27-MDM2 was among the complexes with the best binding energy.

    In plain wordsIn lab computer models, PNC27-MDM2 was among the complexes with the best binding energy.

    Peptide
    PNC-27
    Outcome
    Not applicableMDM2 binding energy
    Study

    n: not reported in source

    DFT and molecular docking
    Outcome group
    Receptor activity and mechanism · Cancer

    Source sentences

    Summary
    Also, molecular docking indicated that the PNC27B-MDM2, PNC28B-MDM2, PNC27-MDM2 and PNC28A-MDM2 complexes show the best binding energy.
    1 context sentence
    Summary · context
    by means of chemical descriptors at the DFT-BHandHLYP level in an aqueous solution, and its intermolecular interactions through molecular docking studies.

    In this study, PNC-27 was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking PNC-27.

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 2Current

    21 Oct 2026, 15:58 UTC

    Study results updated

  2. Version 1

    21 Oct 2026, 12:50 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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