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Study · Not a test of the peptide alone · 2020

3 results

In silico strategy for detailing the binding modes of a novel family of peptides proven as ghrelin receptor agonists.

de la Nuez Veulens A, Rodríguez Fernández RE, Álvarez Ginarte YM, Montero Cabrera LA

Journal of molecular modeling5 Oct 2020Cited by 3 (Europe PMC)

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 study3

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

Studies that did not test the peptide alone3

In this study, GHRP-6 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 GHRP-6.

  1. 01Computer modelNot a test of GHRP-6 aloneIn silicoMechanism

    In docking models, GHRP‑6 and the other studied peptides showed superposition of their N-terminal and first aromatic residue.

    In plain wordsIn computer models, GHRP‑6 and other peptides showed overlapping positions of their N-terminal and first aromatic residue.

    Peptide
    GHRP-6
    Outcome
    Not applicableDocked peptide orientation
    Study

    n: not reported in source

    GHS-R1a molecular docking and dynamics
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    Docking was used to estimate peptide orientations in the binding site of the best model, observing a superposition of its N-terminal and its first aromatic residue.
    1 context sentence
    Summary · context
    In this work, an in silico strategy was developed for describing and assessing the binding modes of A228 and A233 to GHS-R1a (ghrelin receptor) comparing it with ghrelin and GHRP-6 peptides.

    In this study, GHRP-6 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 GHRP-6.

  2. 02Computer modelNot a test of GHRP-6 aloneIn silicoMechanism

    In computer models, GHRP‑6 shared a binding mode involving N-terminal interaction with E124 and aromatic interaction with the receptor aromatic cluster.

    In plain wordsIn computer models, GHRP‑6 shared receptor contacts with the other studied peptides.

    Peptide
    GHRP-6
    Outcome
    Not applicableShared receptor binding mode
    Study

    n: not reported in source

    GHS-R1a molecular docking and dynamics
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    Despite of the structural differences, the studied peptides share a common binding mode; the N-terminal interacts with E124 and the aromatic residue close to it, with the aromatic cluster (F279, F309, and F312).
    1 context sentence
    Summary · context
    In this work, an in silico strategy was developed for describing and assessing the binding modes of A228 and A233 to GHS-R1a (ghrelin receptor) comparing it with ghrelin and GHRP-6 peptides.

    In this study, GHRP-6 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 GHRP-6.

  3. 03Computer modelNot a test of GHRP-6 aloneIn silicoMechanism

    In computer models including GHRP‑6, the proposed pharmacophore contained a charged amine and aromatic ring approximately 0.79 nm apart.

    In plain wordsIn computer models including GHRP‑6, a proposed binding pattern placed an amine and aromatic ring approximately 0.79 nm apart.

    Peptide
    GHRP-6
    Outcome
    Not applicablePharmacophore feature spacing
    Study

    n: not reported in source

    GHS-R1a molecular docking and dynamics
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Measurements

    Pharmacophore distance
    ≈ 0.79 nm
    proposed pharmacophore

    Source sentences

    Summary
    A preliminary pharmacophore model, consisting in a positive charged amine and an aromatic ring at an approximate distance of 0.79 nm, can be proposed.
    1 context sentence
    Summary · context
    In this work, an in silico strategy was developed for describing and assessing the binding modes of A228 and A233 to GHS-R1a (ghrelin receptor) comparing it with ghrelin and GHRP-6 peptides.

    In this study, GHRP-6 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 GHRP-6.

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

    9 Oct 2026, 03:13 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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