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Study · In vitro (cell-free) · 1997

2 results

Mapping the binding site of thymosin beta4 on actin by competition with G-actin binding proteins indicates negative co-operativity between binding sites located on opposite subdomains of actin.

Ballweber E, Hannappel E, Huff T, Mannherz HG

The Biochemical journal1 Nov 1997Cited by 26 (Europe PMC)

PMID9581557 (opens in a new tab)PMCIDPMC1218858 (opens in a new tab)DOI10.1042/bj3270787 (opens in a new tab)PepBankPUB-09581557
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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

    In cell-free assays, thymosin beta‑4 competed with intact gelsolin and gelsolin segment 1 for actin binding, so it binds close to or at the segment 1 binding site.

    In plain wordsIn lab tests, thymosin beta‑4 competed with gelsolin for actin, which suggests it binds near the gelsolin binding site.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableCompetition with gelsolin segment 1 for actin binding
    Study

    n: not reported in source

    Purified actin with DNase I, gelsolin or gelsolin segment 1
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Competition of thymosin beta4 for actin binding was observed in the presence of intact gelsolin or the N-terminal gelsolin fragment, segment 1, indicating that thymosin beta4 binds to a site close to or identical with the gelsolin segment 1-binding site.
    1 context sentence
    Summary · context
    The binding region of thymosin beta4 was determined by analysing the binding of thymosin beta4 to actin complexed with DNase I, gelsolin or gelsolin segment 1.
  2. 02LabIn vitro (cell-free)Mechanism

    In cell-free assays, the actin-DNase I-thymosin beta‑4 complex formed only from the cross-linked actin-thymosin beta‑4 complex, so DNase I binding dissociates thymosin beta‑4 from actin.

    In plain wordsIn lab tests, DNase I pushed thymosin beta‑4 off actin unless the two were chemically cross-linked first.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableTernary complex of actin, DNase I and thymosin beta 4
    Study

    n: not reported in source

    Purified actin with DNase I, gelsolin or gelsolin segment 1
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    The ternary complex of actin-DNase I-thymosin beta4 was obtained only when using the chemically cross-linked actin-thymosin beta4 complex, indicating that thymosin beta4 is dissociated by the binding of DNase I to actin.
    1 context sentence
    Summary · context
    The binding region of thymosin beta4 was determined by analysing the binding of thymosin beta4 to actin complexed with DNase I, gelsolin or gelsolin segment 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 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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