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Study · Not a test of the peptide alone · 2017

3 results

Production of Nα-acetyl Tα1-HSA through in vitro acetylation by RimJ.

Chen J, Li H, Wang T, Sun S, Liu J, Chen J

Oncotarget14 Aug 2017Cited by 3 (Europe PMC)

PMID29221124 (opens in a new tab)PMCIDPMC5707018 (opens in a new tab)DOI10.18632/oncotarget.20259 (opens in a new tab)PepBankPUB-29221124
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Summary

Thymosin alpha 1 (Tα1) is an important immunomodulating agent with various clinical applications. The natural form of Tα1 is Nα -acetylated, which was supposed to be related to in vivo stability of the hormone. In this study, fusion protein Tα1-HSA was constructed and expressed in Pichia pastoris. RimJ, a Nα -acetyltransferase from E.coli, was also overexpressed and purified to homogeneity. In vitro acetylation of Tα1-HSA in the presence of RimJ and acetyl coenzyme A resulted in Nα -acetyl Tα1-HSA. The Nα -acetylation was determined by LC-MS/MS. Kinetic assay indicated that RimJ had a higher affinity to desacetyl Tα1 than to Tα1-HSA. Bioactivity assay revealed fully retained activity of Tα1 when the hormone was connected to the N-terminus of the fusion protein, while the activity was compromised in our previously constructed HSA-Tα1. With fully retained activity and N-terminal acetylation, Nα -acetyl Tα1-HSA was expected to be a more promising pharmaceutical agent than Tα1.
CC BYText from Europe PMC. Highlighted sentences are the source of results.

Results from this study3

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

Studies that did not test the peptide alone3

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

    In vitro acetylation of the fusion protein Tα1-HSA with RimJ and acetyl coenzyme A produced N-alpha-acetyl Tα1-HSA.

    In plain wordsIn lab tests, an enzyme added an acetyl group to a thymosin alpha‑1 fusion protein.

    Peptide
    Thymosin alpha-1
    Outcome
    Not applicableIn vitro N-alpha-acetylation of Tα1-HSA by RimJ
    Study

    n: not reported in source

    Recombinant Tα1-HSA fusion protein
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    In vitro acetylation of Tα1-HSA in the presence of RimJ and acetyl coenzyme A resulted in Nα -acetyl Tα1-HSA.

    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 a kinetic assay, RimJ had a higher affinity to desacetyl Tα1 than to Tα1-HSA.

    In plain wordsIn lab tests, the enzyme RimJ bound the free peptide more strongly than the thymosin alpha‑1 fusion protein.

    Peptide
    Thymosin alpha-1
    Outcome
    Not applicableRimJ affinity for desacetyl Tα1 versus Tα1-HSA
    Study

    n: not reported in source

    Recombinant Tα1-HSA fusion protein
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    Kinetic assay indicated that RimJ had a higher affinity to desacetyl Tα1 than to Tα1-HSA.

    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.

  3. 03LabNot a test of Thymosin alpha-1 aloneOther designActivity measurement

    In a bioactivity assay, Tα1 kept its full activity when connected to the N-terminus of HSA, while activity was compromised in the earlier HSA-Tα1 construct.

    In plain wordsIn lab tests, thymosin alpha‑1 kept its activity when joined at the start of the fusion protein, but lost some at the end.

    Peptide
    Thymosin alpha-1
    Outcome
    Not applicableBioactivity of Tα1 fused to HSA
    Study

    n: not reported in source

    Recombinant Tα1-HSA fusion protein
    Comparator
    HSA-Tα1
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    Bioactivity assay revealed fully retained activity of Tα1 when the hormone was connected to the N-terminus of the fusion protein, while the activity was compromised in our previously constructed HSA-Tα1.

    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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