Interactions of beta-thymosins, thymosin beta 4-sulfoxide, and N-terminally truncated thymosin beta 4 with actin studied by equilibrium centrifugation, chemical cross-linking and viscometry.

Huff T, Zerzawy D, Hannappel E

European journal of biochemistry1 Jun 1995Cited by 43 (Europe PMC)

PMID7607239DOI10.1111/j.1432-1033.1995.tb20606.xPepBankPUB-07607239

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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

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

01LabIn vitro (cell-free)Activity measurement
In lab tests, thymosin beta‑4 bound G-actin from bovine heart with an apparent dissociation constant of 2.5 microM.
In plain wordsIn lab tests, thymosin beta‑4 bound actin from bovine heart with a measured binding strength.
Peptide
Thymosin beta-4 (human)
Outcome
Not applicableApparent dissociation constant for bovine heart actin
Study
n: not reported in source
purified G-actin
Outcome group
Receptor activity and mechanism · Pharmacology
Studied dose
Dose not stated · in vitroAs given in this study.
Measurements
Apparent dissociation constant
2.5 µM
thymosin beta 4, bovine heart actin
Source sentences
Summary
The apparent dissociation constants for actin from bovine heart and beta-thymosins were 2.5, 0.1, and 2.7 microM for thymosin beta 4, [Ala1]beta 4(beta Ala4), and beta 10, respectively.
1 context sentence(design, population, supporting numbers)
Summary · context
Instead of labeling actin we employed equilibrium centrifugation of unlabeled G-actin, viscometry, and chemical cross-linking to investigate the interactions with several beta-thymosins, oxidized thymosin beta 4 and N-terminally truncated beta 4.
Report a problemFND-0760723901
02LabIn vitro (cell-free)Activity measurement
In lab tests, thymosin beta‑4 had a comparable apparent dissociation constant for G-actin from rabbit skeletal muscle.
In plain wordsIn lab tests, thymosin beta‑4 bound rabbit muscle actin about as strongly as bovine heart actin.
Peptide
Thymosin beta-4 (human)
Outcome
Not applicableApparent dissociation constant for rabbit skeletal muscle actin
Study
n: not reported in source
purified G-actin
Outcome group
Receptor activity and mechanism · Pharmacology
Studied dose
Dose not stated · in vitroAs given in this study.
Source sentences
Summary
Comparable apparent dissociation constants were obtained for the interaction of G-actin from rabbit skeletal muscle and thymosin beta 4 or beta Ala4.
1 context sentence(design, population, supporting numbers)
Summary · context
Instead of labeling actin we employed equilibrium centrifugation of unlabeled G-actin, viscometry, and chemical cross-linking to investigate the interactions with several beta-thymosins, oxidized thymosin beta 4 and N-terminally truncated beta 4.
Report a problemFND-0760723902
03LabIn vitro (cell-free)Activity measurement
In lab tests, the apparent dissociation constant of the actin/thymosin beta‑4 complex generated from a preformed actin/DNase-I complex was 160 microM.
In plain wordsIn lab tests, the complex formed from actin already bound to DNase I and thymosin beta‑4 had an apparent dissociation constant of 160 microM.
Peptide
Thymosin beta-4 (human)
Outcome
Not applicableDissociation constant of actin/thymosin beta 4 complex from preformed actin/DNase-I complex
Study
n: not reported in source
purified G-actin
Outcome group
Receptor activity and mechanism · Pharmacology
Studied dose
Dose not stated · in vitroAs given in this study.
Measurements
Apparent dissociation constant
160 µM
actin/thymosin beta 4 complex from preformed actin/DNase-I complex
Source sentences
Summary
While the apparent dissociation constant of the actin/thymosin beta 4 complex generated from a preformed actin/DNase-I complex is 160 microM, a fivefold excess of DNase I over the preformed actin/thymosin-beta 4 complex is necessary to observe a comparable dissociation constant.
1 context sentence(design, population, supporting numbers)
Summary · context
Instead of labeling actin we employed equilibrium centrifugation of unlabeled G-actin, viscometry, and chemical cross-linking to investigate the interactions with several beta-thymosins, oxidized thymosin beta 4 and N-terminally truncated beta 4.
Report a problemFND-0760723903

Studies that did not test the peptide alone4

In this study, Thymosin beta-4 (human) 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 beta-4 (human).

04LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Activity measurement
In lab tests, all studied beta-thymosins interacted with G-actin in a bimolecular complex and inhibited polymerization to F-actin under high salt.
In plain wordsIn lab tests, all the beta-thymosins studied bound actin and blocked it from assembling under high salt.
Peptide
Thymosin beta-4 (human)
Outcome
DecreaseG-actin binding and inhibition of polymerization by beta-thymosins
Study
n: not reported in source
purified G-actin
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
All beta-thymosins studied interact with G-actin in a bimolecular complex and inhibit the polymerization to F-actin under high salt conditions.
1 context sentence(design, population, supporting numbers)
Summary · context
Instead of labeling actin we employed equilibrium centrifugation of unlabeled G-actin, viscometry, and chemical cross-linking to investigate the interactions with several beta-thymosins, oxidized thymosin beta 4 and N-terminally truncated beta 4.
In this study, Thymosin beta-4 (human) 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 beta-4 (human).
Report a problemFND-0760723904
05LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Activity measurement
In lab tests, oxidation at Met6 or truncation of 6 or 12 N-terminal residues of thymosin beta‑4 raised apparent dissociation constants to 38-53 microM.
In plain wordsIn lab tests, oxidized or shortened thymosin beta‑4 bound actin more weakly than the full peptide.
Peptide
Thymosin beta-4 (human)
Outcome
IncreaseActin binding of oxidized and N-terminally truncated thymosin beta 4
Study
n: not reported in source
purified G-actin
Outcome group
Receptor activity and mechanism · Pharmacology
Measurements
Apparent dissociation constant
38 to 53 µM
beta 4-sulfoxide, beta 4-(7-43), beta 4-(13-43)
Source sentences
Summary
Oxidation of thymosin beta 4 at Met6 (beta 4-sulfoxide) as well as truncation of 6 [beta 4-(7-43)] or 12 [beta 4-(13-43)] amino acid residues from the N-terminus increase apparent dissociation constants to 38-53 microM.
1 context sentence(design, population, supporting numbers)
Summary · context
Instead of labeling actin we employed equilibrium centrifugation of unlabeled G-actin, viscometry, and chemical cross-linking to investigate the interactions with several beta-thymosins, oxidized thymosin beta 4 and N-terminally truncated beta 4.
In this study, Thymosin beta-4 (human) 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 beta-4 (human).
Report a problemFND-0760723905
06LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Activity measurement
In lab tests, truncation of the first 23 residues of thymosin beta‑4 abolished interaction with G-actin completely.
In plain wordsIn lab tests, a thymosin beta‑4 piece missing its first 23 residues did not bind actin at all.
Peptide
Thymosin beta-4 (human)
Outcome
DecreaseActin interaction of beta 4-(24-43)
Study
n: not reported in source
purified G-actin
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
Truncation of the first 23 amino acid residues [beta 4-(24-43)] abolishes interaction with G-actin completely.
1 context sentence(design, population, supporting numbers)
Summary · context
Instead of labeling actin we employed equilibrium centrifugation of unlabeled G-actin, viscometry, and chemical cross-linking to investigate the interactions with several beta-thymosins, oxidized thymosin beta 4 and N-terminally truncated beta 4.
In this study, Thymosin beta-4 (human) 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 beta-4 (human).
Report a problemFND-0760723906
07LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Activity measurement
In lab tests, only thymosin beta‑4-sulfoxide and not the truncated forms inhibited actin polymerization, and only at a 20-fold higher concentration than thymosin beta‑4.
In plain wordsIn lab tests, only oxidized thymosin beta‑4 blocked actin assembly, and it needed a much higher concentration than thymosin beta‑4.
Peptide
Thymosin beta-4 (human)
Outcome
MixedInhibition of actin polymerization by sulfoxide and truncated forms
Study
n: not reported in source
purified G-actin
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
In spite of comparable apparent dissociation constants between actin and thymosin beta 4-sulfoxide or beta 4-(7-43) or beta 4-(13-43), only beta 4-sulfoxide and not the truncated beta-thymosins inhibits actin polymerization, however, only at a 20-fold higher concentration than beta 4.
1 context sentence(design, population, supporting numbers)
Summary · context
Instead of labeling actin we employed equilibrium centrifugation of unlabeled G-actin, viscometry, and chemical cross-linking to investigate the interactions with several beta-thymosins, oxidized thymosin beta 4 and N-terminally truncated beta 4.
In this study, Thymosin beta-4 (human) 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 beta-4 (human).
Report a problemFND-0760723907

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.

Version 2Current
13 Oct 2026, 01:52 UTC
Study results updated
Version 1
12 Oct 2026, 18:17 UTC
First added · source update from Europe PMC

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