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Bicyclic Engineered Sortase A Performs Transpeptidation under Denaturing Conditions.

Sebastian Kiehstaller1, George H Hutchins2,3, Alessia Amore2,3

  • 1Incircular BV, De Boelelaan 1108, 1081 HZ Amsterdam, The Netherlands.

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|May 29, 2023
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Summary
This summary is machine-generated.

Researchers stabilized Sortase A, an enzyme crucial for bioconjugation, using a novel protein cyclization method. The stabilized enzyme retains function under harsh thermal and chemical conditions, expanding its biotechnological applications.

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Area of Science:

  • Biochemistry
  • Protein Engineering
  • Biotechnology

Background:

  • Enzymes are vital for biotechnological and biomedical applications.
  • Harsh conditions like thermal and chemical stress limit enzyme function, hindering applications.
  • Sortase A, a transpeptidase, is widely used for protein and peptide bioconjugation but is sensitive to stress.

Purpose of the Study:

  • To enhance the stability of an activity-enhanced Sortase A variant.
  • To enable Sortase A function under challenging thermal and chemical conditions.
  • To expand the scope of Sortase A-mediated bioconjugation reactions.

Main Methods:

  • Employed the in situ protein cyclization (INCYPRO) approach.
  • Introduced three spatially aligned, solvent-exposed cysteines into Sortase A.
  • Attached a triselectrophilic cross-linker to create a bicyclic enzyme.

Main Results:

  • The bicyclic INCYPRO Sortase A exhibited retained activity at elevated temperatures.
  • The stabilized enzyme remained active in the presence of chemical denaturants.
  • Wild-type and activity-enhanced Sortase A were inactive under these conditions.

Conclusions:

  • The INCYPRO approach successfully stabilized Sortase A against thermal and chemical stress.
  • Stabilized Sortase A broadens the applicability of bioconjugation under demanding conditions.
  • This method offers a pathway for engineering robust enzymes for industrial biotechnology.