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Study · In vitro (cell-free) · 1996

2 results

The N-terminal sequences (5-20) of thymosin beta 4 binds to monomeric actin in an alpha-helical conformation.

Feinberg J, Heitz F, Benyamin Y, Roustan C

Biochemical and biophysical research communications1 May 1996Cited by 11 (Europe PMC)

PMID8630056 (opens in a new tab)DOI10.1006/bbrc.1996.0709 (opens in a new tab)PepBankPUB-08630056
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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

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

  1. 01LabIn vitro (cell-free)Mechanism

    The synthetic N-terminal peptide of thymosin beta‑4 is unstructured in solution and becomes folded at medium trifluoroethanol concentrations below 30%.

    In plain wordsIn lab tests, the start of thymosin beta‑4 had no fixed shape alone and folded when a helix-promoting solvent was added.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableConformation of the N-terminal peptide in solution and with TFE
    Study

    n: not reported in source

    synthetic peptide and purified actin
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Measurements

    TFE concentration for folding
    < 30%
    N-terminal peptide

    Source sentences

    Summary
    The peptide is unstructured in solution, and becomes folded at medium TFE concentrations, below 30%.
    2 context sentences
    Summary · context
    The N-terminal part of thymosin beta 4, including the 5-20 sequences, is implicated in binding to monomeric actin.
    Summary · context
    The corresponding peptide was synthesized and its conformation studied by CD.
  2. 02LabIn vitro (cell-free)Activity measurement

    The apparent affinity of the synthetic peptide for monomeric actin was increased by an order of magnitude in the presence of trifluoroethanol.

    In plain wordsIn lab tests, the thymosin beta‑4 start peptide bound actin about ten times more strongly when it was folded.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    IncreaseApparent affinity of the peptide for monomeric actin with TFE
    Study

    n: not reported in source

    synthetic peptide and purified actin
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    We report here that the apparent affinity of the synthetic peptide to monomeric actin is increased by an order of magnitude in the presence of TFE, which implies that the peptide adopts a folded conformation needed for accurate interaction.
    2 context sentences
    Summary · context
    The N-terminal part of thymosin beta 4, including the 5-20 sequences, is implicated in binding to monomeric actin.
    Summary · context
    The corresponding peptide was synthesized and its conformation studied by CD.

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

    13 Oct 2026, 01:52 UTC

    Study results updated

  2. Version 1

    12 Oct 2026, 18:17 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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