Sortase-mediated backbone cyclization of proteins and peptides

Biol Chem. 2015 Apr;396(4):283-93. doi: 10.1515/hsz-2014-0260.

Abstract

Backbone cyclization has a profound impact on the biological activity and thermal and proteolytic stability of proteins and peptides. Chemical methods for cyclization are not always feasible, especially for large peptides or proteins. Recombinant Staphylococcus aureus sortase A shows potential as a new tool for the cyclization of both proteins and peptides. In this review, the scope and background of the sortase-mediated cyclization are discussed. High efficiency, versatility, and easy access make sortase A a promising cyclization tool, both for recombinant and chemo-enzymatic production methods.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Aminoacyltransferases / chemistry
  • Aminoacyltransferases / metabolism*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism*
  • Carbohydrate Sequence
  • Cyclization
  • Cysteine Endopeptidases / chemistry
  • Cysteine Endopeptidases / metabolism*
  • Models, Molecular
  • Molecular Sequence Data
  • Peptides / chemistry
  • Peptides / metabolism*
  • Peptides, Cyclic / chemistry
  • Peptides, Cyclic / metabolism*
  • Peptidoglycan / chemistry
  • Peptidoglycan / metabolism
  • Protein Conformation
  • Protein Engineering
  • Proteins / chemistry
  • Proteins / metabolism*
  • Recombinant Proteins / metabolism
  • Staphylococcus aureus / enzymology*
  • Staphylococcus aureus / metabolism

Substances

  • Bacterial Proteins
  • Peptides
  • Peptides, Cyclic
  • Peptidoglycan
  • Proteins
  • Recombinant Proteins
  • Aminoacyltransferases
  • sortase A
  • Cysteine Endopeptidases