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Study · Not a test of the peptide alone · 2015

2 results

Thymosin α1 inserts N terminus into model membranes assuming a helical conformation.

Nepravishta R, Mandaliti W, Eliseo T, Sinibaldi Vallebona P, Pica F, Garaci E, Paci M

Expert opinion on biological therapy2 Feb 2015Cited by 12 (Europe PMC)

PMID25642593 (opens in a new tab)DOI10.1517/14712598.2015.1009034 (opens in a new tab)PepBankPUB-25642593
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, Thymosin alpha-1 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 Thymosin alpha-1.

  1. 01LabNot a test of Thymosin alpha-1 aloneIn vitro (cell-free)Mechanism

    In the presence of sodium dodecyl sulfate micelles, thymosin alpha‑1 assumed a helical conformation with a structural break around residues 9 and 14.

    In plain wordsIn lab tests with model membranes, thymosin alpha‑1 folded into a helix, which it does not do in water.

    Peptide
    Thymosin alpha-1
    Outcome
    Not applicableTα1 conformation in SDS micelles
    Study

    n: not reported in source

    Sodium dodecyl sulfate micelles
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    Tα1 assumes a helical conformation in the presence of sodium dodecyl sulfate micelles, showing a helical fold with a structural break around residues 9 and 14.
    1 context sentence
    Summary · context
    The folding and interaction of Tα1 with sodium dodecyl sulfate micelles was monitored by NMR and CD spectroscopy techniques.

    In this study, Thymosin alpha-1 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 Thymosin alpha-1.

  2. 02LabNot a test of Thymosin alpha-1 aloneIn vitro (cell-free)Mechanism

    Paramagnetic NMR relaxation showed that thymosin alpha‑1 inserts into the hydrophobic region of the micelles through residues 1-5 of its N-terminal end.

    In plain wordsIn lab tests with model membranes, the first five amino acids of thymosin alpha‑1 went into the oily core of the membrane model.

    Peptide
    Thymosin alpha-1
    Outcome
    Not applicableTα1 insertion into micelles
    Study

    n: not reported in source

    Sodium dodecyl sulfate micelles
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    Moreover, by paramagnetic NMR relaxation it was found that Tα1 is inserted in the hydrophobic region of the micelles by the residues 1 - 5 of the N-terminal end.
    1 context sentence
    Summary · context
    The folding and interaction of Tα1 with sodium dodecyl sulfate micelles was monitored by NMR and CD spectroscopy techniques.

    In this study, Thymosin alpha-1 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 Thymosin alpha-1.

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, 08:55 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, 03:02 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

Publication types

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