Skip to content

Study · Not a test of the peptide alone · 2013

2 results

Effect of proline mutations on the monomer conformations of amylin.

Chiu CC, Singh S, de Pablo JJ

Biophysical journal1 Sept 2013Cited by 45 (Europe PMC)

PMID24010666 (opens in a new tab)PMCIDPMC3762349 (opens in a new tab)DOI10.1016/j.bpj.2013.07.029 (opens in a new tab)PepBankPUB-24010666
Source linkPubMedAsk about this study
Jump to 2 results

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, Pramlintide (Symlin) 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 Pramlintide (Symlin).

  1. 01Computer modelNot a test of Pramlintide (Symlin) aloneIn silicoMechanism

    In molecular simulations, all three pramlintide proline substitutions were required to inhibit beta conformations.

    In plain wordsComputer simulations showed that all three pramlintide proline substitutions were required to inhibit beta conformations.

    Peptide
    Pramlintide (Symlin)
    Outcome
    DecreaseBeta conformation inhibition
    Study

    n: not reported in source

    Molecular simulations of hIAPP monomers
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    More importantly, we find that all three proline substitutions of pramlintide are required to inhibit β conformations and stabilize the α-helical conformation.
    1 context sentence
    Summary · context
    In this work, we use molecular simulations and bias-exchange metadynamics to investigate the effect of proline substitutions on the conformation of the hIAPP monomer.

    In this study, Pramlintide (Symlin) 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 Pramlintide (Symlin).

  2. 02Computer modelNot a test of Pramlintide (Symlin) aloneIn silicoMechanism

    In molecular simulations, all three pramlintide proline substitutions were required to stabilize the alpha-helical conformation.

    In plain wordsComputer simulations showed that all three pramlintide proline substitutions were required to stabilize the alpha-helical conformation.

    Peptide
    Pramlintide (Symlin)
    Outcome
    IncreaseAlpha-helical conformation stabilization
    Study

    n: not reported in source

    Molecular simulations of hIAPP monomers
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    More importantly, we find that all three proline substitutions of pramlintide are required to inhibit β conformations and stabilize the α-helical conformation.
    1 context sentence
    Summary · context
    In this work, we use molecular simulations and bias-exchange metadynamics to investigate the effect of proline substitutions on the conformation of the hIAPP monomer.

    In this study, Pramlintide (Symlin) 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 Pramlintide (Symlin).

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

    22 Oct 2026, 02:26 UTC

    Study results updated

  2. Version 1

    21 Oct 2026, 18:59 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.