Skip to content

Study · In vitro (cell-free) · 1994

5 results

Interaction of G-actin with thymosin beta 4 and its variants thymosin beta 9 and thymosin beta met9.

Jean C, Rieger K, Blanchoin L, Carlier MF, Lenfant M, Pantaloni D

Journal of muscle research and cell motility1 Jun 1994Cited by 37 (Europe PMC)

PMID7929793 (opens in a new tab)DOI10.1007/bf00123480 (opens in a new tab)PepBankPUB-07929793
Publisher pagePubMedAsk about this study
Jump to 5 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 study5

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

  1. 01LabIn vitro (cell-free)Activity measurement

    In purified protein assays, thymosin beta‑4 inhibited polymerization of ATP-actin with a KD of 2 microM, compared with 0.7-0.8 microM for thymosin beta 9 and thymosin beta met9.

    In plain wordsIn lab tests, thymosin beta‑4 held back actin from forming filaments, with a binding constant of 2 microM.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableInhibition of ATP-actin polymerization (KD)
    Study

    n: not reported in source

    Purified G-actin in vitro
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Measurements

    KD
    2 microM
    thymosin beta 4, ATP-actin polymerization inhibition

    Source sentences

    Summary
    inhibit polymerization of ATP-actin with identical KDs of 0.7-0.8 microM (as compared to 2 +/- 0.3 microM for thymosin beta 4)
    1 context sentence
    Summary · context
    The possible function of these peptides has been investigated by comparing the actin binding properties of these beta-thymosins.
  2. 02LabIn vitro (cell-free)Activity measurement

    In purified protein assays, thymosin beta‑4 bound ADP-G-actin with a 100-fold lower affinity than ATP-G-actin.

    In plain wordsIn lab tests, thymosin beta‑4 bound ADP-actin far more weakly than ATP-actin, about 100-fold lower.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    DecreaseAffinity for ADP-G-actin versus ATP-G-actin
    Study

    n: not reported in source

    Purified G-actin in vitro
    Comparator
    ATP-G-actin
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Measurements

    Affinity ratio ADP-G-actin to ATP-G-actin
    100 fold lower
    thymosin beta 4

    Source sentences

    Summary
    like thymosin beta 4, they bound to ADP-G-actin with a 100-fold lower affinity than to ATP-G-actin.
    1 context sentence
    Summary · context
    The possible function of these peptides has been investigated by comparing the actin binding properties of these beta-thymosins.
  3. 03LabIn vitro (cell-free)Activity measurement

    In purified protein assays, oxidation of methionine-6 into methionine sulfoxide weakened the interaction of thymosin beta‑4 with G-actin 20-fold.

    In plain wordsIn lab tests, oxidising one amino acid (methionine-6) of thymosin beta‑4 weakened its binding to actin 20-fold.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    DecreaseEffect of methionine-6 oxidation on G-actin binding
    Study

    n: not reported in source

    Purified G-actin in vitro
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Measurements

    Interaction weakening
    20 fold
    thymosin beta 4 after methionine-6 oxidation

    Source sentences

    Summary
    The interaction of thymosin beta 4 and thymosin beta met9 with G-actin was weakened 20-fold upon oxidation of methionine-6 into methionine sulfoxide.
    1 context sentence
    Summary · context
    The possible function of these peptides has been investigated by comparing the actin binding properties of these beta-thymosins.
  4. 04LabIn vitro (cell-free)Activity measurement

    In purified protein assays, binding of thymosin beta‑4 to G-actin was accompanied by a 15% increase in actin tryptophan fluorescence and a 10 nm emission blue shift, with methionine-6 important for this effect.

    In plain wordsIn lab tests, thymosin beta‑4 binding to actin raised actin fluorescence by 15% and shifted its emission by 10 nm.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    IncreaseActin tryptophan fluorescence change on binding
    Study

    n: not reported in source

    Purified G-actin in vitro
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Measurements

    Fluorescence intensity increase
    15%
    actin tryptophans
    Emission blue shift
    10 nm
    actin tryptophans

    Source sentences

    Summary
    Binding of thymosin beta 4 to G-actin was accompanied by a 15% increase in the fluorescence intensity of actin tryptophans, and a 10 nm emission blue shift. Methionine-6 played an important role in this effect.
    1 context sentence
    Summary · context
    The possible function of these peptides has been investigated by comparing the actin binding properties of these beta-thymosins.
  5. 05LabIn vitro (cell-free)Activity measurement

    In stopped-flow assays, thymosin beta‑4 binding to G-actin was bimolecular, with association and dissociation rate constants of approximately 1.5 microM-1 s-1 and 2 s-1 under physiological conditions.

    In plain wordsIn lab tests, thymosin beta‑4 bound actin in a two-molecule reaction, with rate constants of about 1.5 per microM per second and 2 per second.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableBinding kinetics of thymosin beta 4 to G-actin
    Study

    n: not reported in source

    Purified G-actin in vitro
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Measurements

    Association rate constant
    ≈ 1.5 microM-1 s-1
    physiological conditions
    Dissociation rate constant
    ≈ 2 s-1
    physiological conditions

    Source sentences

    Summary
    The reaction was bimolecular, with association and dissociation rate constants of approximately 1.5 microM-1 s-1 and 2 s-1 respectively, under physiological conditions.
    1 context sentence
    Summary · context
    The possible function of these peptides has been investigated by comparing the actin binding properties of these beta-thymosins.

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.

PepBank is a research reference. Talk to a doctor before you use any peptide.