Generation of antibody-drug conjugates by proximity-driven acyl transfer and sortase-mediated ligation

Org Biomol Chem. 2024 Dec 18;23(1):188-196. doi: 10.1039/d4ob01624f.

Abstract

We report a sortase-based site-specific antibody-drug conjugation strategy, which involves an affinity peptide-directed acyl transfer reaction and sortase-mediated peptide ligation. Through the affinity peptide-mediated acyl transfer reaction, an LPXTG-containing peptide is conjugated to a specific Lys side chain of an antibody. Under the assistance of sortase, a protein drug bearing a GG motif reacts specifically with the LPXTG moiety to produce an antibody-drug conjugate. Our strategy for antibody conjugation can be applied not only to chemically synthesized drugs, but also to biologically expressed proteins, and will provide a new sortase-based strategy for the preparation of antibody-drug conjugates.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acylation
  • Aminoacyltransferases* / chemistry
  • Aminoacyltransferases* / metabolism
  • Bacterial Proteins* / chemistry
  • Bacterial Proteins* / metabolism
  • Cysteine Endopeptidases* / chemistry
  • Cysteine Endopeptidases* / metabolism
  • Immunoconjugates* / chemistry
  • Peptides / chemistry

Substances

  • Aminoacyltransferases
  • Immunoconjugates
  • Cysteine Endopeptidases
  • Bacterial Proteins
  • sortase A
  • Peptides