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Study · Not a test of the peptide alone · 2013

2 results

Generation of mature Nα-terminal acetylated thymosin α 1 by cleavage of recombinant prothymosin α.

Liu B, Gong X, Chang S, Sun P, Wu J

TheScientificWorldJournal28 Oct 2013Cited by 3 (Europe PMC)

Summary

N(α)-terminal acetylation of peptides plays an important biological role but is rarely observed in prokaryotes. N(α)-terminal acetylated thymosin α1 (Tα1), a 28-amino-acid peptide, is an immune modifier that has been used in the clinic to treat hepatitis B and C virus (HBV/HCV) infections. We previously documented N(α)-terminal acetylation of recombinant prothymosin α (ProTα) in E. coli. Here we present a method for production of N(α)-acetylated Tα1 from recombinant ProTα. The recombinant ProTα was cleaved by human legumain expressed in Pichia pastoris to release Tα1 in vitro. The N(α)-acetylated Tα1 peptide was subsequently purified by reverse phase and cation exchange chromatography. Mass spectrometry indicated that the molecular mass of recombinant N(α)-acetylated Tα1 was 3108.79 in, which is identical to the mass of N(α)-acetylated Tα1 produced by total chemical synthesis. This mass corresponded to the nonacetylated Tα1 mass with a 42 Da increment. The retention time of recombinant N(α)-acetylated Tα1 and chemosynthetic N(α)-acetylated Tα1 were both 15.4 min in RP-high performance liquid chromatography (HPLC). These data support the use of an E. coli expression system for the production of recombinant human N(α)-acetylated Tα1 and also will provide the basis for the preparation of recombinant acetylated peptides in E. coli.
CC BYText from Europe PMC. Highlighted sentences are the source of results.

Results from this study2

No result from this study comes from a test of the peptide.

Studies that did not test the peptide alone2

In this study, Thymosin alpha-1 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 alpha-1.

  1. 01LabNot a test of Thymosin alpha-1 aloneIn vitro (cell-free)Other

    Mass spectrometry showed that recombinant Nα-acetylated thymosin α1 had a molecular mass identical to that of the chemically synthesized peptide.

    In plain wordsIn lab tests, thymosin α1 made in bacteria had the same mass as the chemically made peptide.

    Outcome
    Not applicableMolecular mass of recombinant Nα-acetylated Tα1
    Study

    n: not reported in source

    Comparator
    Chemically synthesized Nα-acetylated Tα1
    Outcome group
    Synthesis and manufacturing · Pharmacology

    Measurements

    molecular mass
    3108.79 Da
    recombinant Nα-acetylated Tα1

    Source sentences

    Summary
    Mass spectrometry indicated that the molecular mass of recombinant N(α)-acetylated Tα1 was 3108.79 in, which is identical to the mass of N(α)-acetylated Tα1 produced by total chemical synthesis.
    1 context sentence
    Summary · context
    The recombinant ProTα was cleaved by human legumain expressed in Pichia pastoris to release Tα1 in vitro.

    In this study, Thymosin alpha-1 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 alpha-1.

  2. 02LabNot a test of Thymosin alpha-1 aloneIn vitro (cell-free)Other

    In RP-HPLC, recombinant and chemosynthetic Nα-acetylated thymosin α1 had the same retention time.

    In plain wordsIn lab tests, thymosin α1 made in bacteria and the chemically made peptide came out of the column at the same time.

    Outcome
    Not applicableRP-HPLC retention time of recombinant Nα-acetylated Tα1
    Study

    n: not reported in source

    Comparator
    Chemically synthesized Nα-acetylated Tα1
    Outcome group
    Synthesis and manufacturing · Pharmacology

    Measurements

    retention time
    15.4 min
    RP-HPLC, both peptides

    Source sentences

    Summary
    The retention time of recombinant N(α)-acetylated Tα1 and chemosynthetic N(α)-acetylated Tα1 were both 15.4 min in RP-high performance liquid chromatography (HPLC).
    1 context sentence
    Summary · context
    The recombinant ProTα was cleaved by human legumain expressed in Pichia pastoris to release Tα1 in vitro.

    In this study, Thymosin alpha-1 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 alpha-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 3Current

    10 Oct 2026, 08:55 UTC

    Study results updated

  2. Version 2

    9 Oct 2026, 03:03 UTC

    Study data updated · source update from Europe PMC

  3. Version 1

    9 Oct 2026, 03:02 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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