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Study · In vitro (cell-free) · 2006

7 results

Thymosin beta4 induces a conformational change in actin monomers.

Dedova IV, Nikolaeva OP, Safer D, De La Cruz EM, dos Remedios CG

Biophysical journal4 Nov 2005Cited by 37 (Europe PMC)

PMID16272441 (opens in a new tab)PMCIDPMC1367123 (opens in a new tab)DOI10.1529/biophysj.105.063081 (opens in a new tab)PepBankPUB-16272441
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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 study7

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

  1. 01LabIn vitro (cell-free)Mechanism

    In actin monomers in solution, thymosin beta(4) binding increased the distance between probes at Gln-41 and Cys-374 by 2 A.

    In plain wordsIn lab tests, thymosin beta(4) binding changed the shape of actin, increasing one measured distance.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    IncreaseDistance between probes at Gln-41 and Cys-374 of actin
    Study

    n: not reported in source

    actin monomers in solution
    Outcome group
    Receptor activity and mechanism · Musculoskeletal
    Studied dose
    Dose not stated

    Measurements

    Distance change Gln-41 to Cys-374
    2 A
    actin monomers with tbeta(4)

    Source sentences

    Summary
    Using fluorescence resonance energy transfer spectroscopy we demonstrate that thymosin beta(4) (tbeta(4)) binding induces spatial rearrangements within the small domain (subdomains 1 and 2) of actin monomers in solution.
    1 context sentence
    Summary · context
    Tbeta(4) binding increases the distance between probes attached to Gln-41 and Cys-374 of actin by 2 A and decreases the distance between the purine base of bound ATP (epsilonATP) and Lys-61 by 1.9 A, whereas the distance between Cys-374 and Lys-61 is minimally affected.
  2. 02LabIn vitro (cell-free)Mechanism

    In actin monomers in solution, thymosin beta(4) binding decreased the distance between the purine base of bound ATP and Lys-61 by 1.9 A.

    In plain wordsIn lab tests, thymosin beta(4) binding changed the shape of actin, decreasing one measured distance.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    DecreaseDistance between bound ATP base and Lys-61 of actin
    Study

    n: not reported in source

    actin monomers in solution
    Outcome group
    Receptor activity and mechanism · Musculoskeletal
    Studied dose
    Dose not stated

    Measurements

    Distance change epsilonATP to Lys-61
    −1.9 A
    actin monomers with tbeta(4)

    Source sentences

    Summary
    Using fluorescence resonance energy transfer spectroscopy we demonstrate that thymosin beta(4) (tbeta(4)) binding induces spatial rearrangements within the small domain (subdomains 1 and 2) of actin monomers in solution.
    1 context sentence
    Summary · context
    Tbeta(4) binding increases the distance between probes attached to Gln-41 and Cys-374 of actin by 2 A and decreases the distance between the purine base of bound ATP (epsilonATP) and Lys-61 by 1.9 A, whereas the distance between Cys-374 and Lys-61 is minimally affected.
  3. 03LabIn vitro (cell-free)Mechanism

    In actin monomers in solution, thymosin beta(4) binding minimally affected the distance between Cys-374 and Lys-61.

    In plain wordsIn lab tests, thymosin beta(4) binding hardly changed the distance between two other points on actin.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    No significant changeDistance between Cys-374 and Lys-61 of actin
    Study

    n: not reported in source

    actin monomers in solution
    Outcome group
    Receptor activity and mechanism · Musculoskeletal
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Using fluorescence resonance energy transfer spectroscopy we demonstrate that thymosin beta(4) (tbeta(4)) binding induces spatial rearrangements within the small domain (subdomains 1 and 2) of actin monomers in solution.
    1 context sentence
    Summary · context
    Tbeta(4) binding increases the distance between probes attached to Gln-41 and Cys-374 of actin by 2 A and decreases the distance between the purine base of bound ATP (epsilonATP) and Lys-61 by 1.9 A, whereas the distance between Cys-374 and Lys-61 is minimally affected.
  4. 04LabIn vitro (cell-free)Mechanism

    By differential scanning calorimetry, thymosin beta(4) binding increased the cooperativity of ATP-actin monomer denaturation.

    In plain wordsIn lab tests, thymosin beta(4) binding made actin denature in a more cooperative way.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    IncreaseCooperativity of ATP-actin monomer denaturation
    Study

    n: not reported in source

    actin monomers in solution
    Outcome group
    Receptor activity and mechanism · Musculoskeletal
    Studied dose
    Dose not stated

    Source sentences

    Summary
    By differential scanning calorimetry, tbeta(4) binding increases the cooperativity of ATP-actin monomer denaturation, consistent with conformational rearrangements in the tbeta(4)-actin complex.
  5. 05LabIn vitro (cell-free)Mechanism

    Thymosin beta(4) binding to actin markedly reduced the solvent accessibility of the probe at Gln-41.

    In plain wordsIn lab tests, thymosin beta(4) binding made one site on actin much less open to the surrounding solution.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    DecreaseSolvent accessibility of the probe at Gln-41
    Study

    n: not reported in source

    actin monomers in solution
    Outcome group
    Receptor activity and mechanism · Musculoskeletal
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Changes in fluorescence resonance energy transfer are accompanied by marked reduction in solvent accessibility of the probe at Gln-41, suggesting it forms part of the binding interface.
  6. 06LabIn vitro (cell-free)Mechanism

    In solution, thymosin beta(4) and cofilin compete for actin binding.

    In plain wordsIn lab tests, thymosin beta(4) and cofilin compete to bind actin.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableCompetition between thymosin beta(4) and cofilin for actin binding
    Study

    n: not reported in source

    actin monomers in solution
    Outcome group
    Receptor activity and mechanism · Musculoskeletal
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Tbeta(4) and cofilin compete for actin binding.
  7. 07LabIn vitro (cell-free)Mechanism

    In solution, thymosin beta(4) concentrations that dissociate cofilin from actin did not dissociate the cofilin-DNase I-actin ternary complex.

    In plain wordsIn lab tests, thymosin beta(4) amounts that remove cofilin from actin did not break up the cofilin-DNase I-actin complex.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    No significant changeDissociation of the cofilin-DNase I-actin ternary complex
    Study

    n: not reported in source

    actin monomers in solution
    Outcome group
    Receptor activity and mechanism · Musculoskeletal
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Tbeta(4) concentrations that dissociate cofilin from actin do not dissociate the cofilin-DNase I-actin ternary complex, consistent with the DNase binding loop contributing to high-affinity tbeta(4)-binding.

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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