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Related Experiment Video

Updated: Jun 2, 2026

Single-Step Enrichment of a TAP-Tagged Histone Deacetylase of the Filamentous Fungus Aspergillus nidulans for Enzymatic Activity Assay
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Single-Step Enrichment of a TAP-Tagged Histone Deacetylase of the Filamentous Fungus Aspergillus nidulans for Enzymatic Activity Assay

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Sortase A as a tool for high-yield histatin cyclization.

Jan G M Bolscher1, Menno J Oudhoff, Kamran Nazmi

  • 1Department of Oral Biochemistry, Academic Centre for Dentistry Amsterdam, University of Amsterdam and VU Amsterdam, Gustav Mahlerlaan 3004, 1081 LA, Amsterdam, The Netherlands. j.bolscher@acta.nl

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
|April 29, 2011
PubMed
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This summary is machine-generated.

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Researchers developed a new method using Staphylococcus aureus sortase A enzyme for efficient cyclic peptide production. This technique significantly improves yields and biological activity for peptides like histatin 1, overcoming previous manufacturing challenges.

Area of Science:

  • Biochemistry
  • Peptide Chemistry
  • Enzymology

Background:

  • Cyclic peptides offer superior receptor affinity, biological activity, and stability compared to linear counterparts.
  • Manufacturing challenges, particularly for larger cyclic peptides, have limited their widespread application in biomedical research.

Purpose of the Study:

  • To introduce a novel and efficient enzymatic method for the cyclization of synthetic peptides.
  • To demonstrate the effectiveness of this method for producing large cyclic peptides with enhanced biological activity.

Main Methods:

  • Utilized the peptidyl-transferase activity of Staphylococcus aureus sortase A enzyme.
  • Employed sortase A for the cyclization of linear synthetic precursor peptides, using histatin 1 as a model.
  • Compared yields and biological activity with traditional chemical cyclization methods.

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Last Updated: Jun 2, 2026

Single-Step Enrichment of a TAP-Tagged Histone Deacetylase of the Filamentous Fungus Aspergillus nidulans for Enzymatic Activity Assay
09:07

Single-Step Enrichment of a TAP-Tagged Histone Deacetylase of the Filamentous Fungus Aspergillus nidulans for Enzymatic Activity Assay

Published on: May 1, 2019

Targeted in Situ Mutagenesis of Histone Genes in Budding Yeast
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Published on: January 26, 2017

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Main Results:

  • Sortase-mediated cyclization achieved yields exceeding 90%, a significant improvement over chemical cyclization (≤ 3%).
  • The sortase-cyclized histatin 1 exhibited potent wound closure activity at 10 nM, vastly superior to the linear peptide at 10 μM.
  • Spectroscopic analyses (Circular Dichroism, NMR) indicated no significant conformational changes in solution, suggesting context-dependent structural effects upon receptor binding.

Conclusions:

  • Sortase A-mediated cyclization is a highly efficient and generalizable technology for producing large cyclic peptides.
  • This method overcomes previous limitations in cyclic peptide manufacturing, paving the way for broader biomedical applications.
  • The enhanced biological activity of sortase-cyclized peptides highlights the potential of this approach for drug discovery and development.