Chemical Conjugation to Less Targeted Proteinogenic Amino Acids

Nanna L. Kjaersgaard, Thorbjorn B. Nielsen, Kurt V. Gothelf*

*Corresponding author for this work

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperReviewResearchpeer-review

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Abstract

Protein bioconjugates are in high demand for applications in biomedicine, diagnostics, chemical biology and bionanotechnology. Proteins are large and sensitive molecules containing multiple different functional groups and in particular nucleophilic groups. In bioconjugation reactions it can therefore be challenging to obtain a homogeneous product in high yield. Numerous strategies for protein conjugation have been developed, of which a vast majority target lysine, cysteine and to a lesser extend tyrosine. Likewise, several methods that involve recombinantly engineered protein tags have been reported. In recent years a number of methods have emerged for chemical bioconjugation to other amino acids and in this review, we present the progress in this area.

Original languageEnglish
Article numbere202200245
JournalChemBioChem
Volume23
Issue19
Number of pages14
ISSN1439-4227
DOIs
Publication statusPublished - Oct 2022

Keywords

  • bioconjugation
  • chemical protein labeling
  • protein conjugation
  • protein modifications
  • site-specific conjugation
  • TRYPTOPHAN-CONTAINING PEPTIDES
  • SITE-SPECIFIC PEGYLATION
  • ANTIBODY-DRUG CONJUGATE
  • SELECTIVE BIOCONJUGATION
  • RADICAL TRIFLUOROMETHYLATION
  • TYROSINE BIOCONJUGATION
  • PERIODATE-OXIDATION
  • RHODIUM CARBENOIDS
  • ARGININE RESIDUES
  • ACTIVE-SITE

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