Expanding the chemical diversity of M13 bacteriophage

Grace L. Allen, Ashley K. Grahn, Katerina Kourentzi, Richard C. Willson, Sean Waldrop, Jiantao Guo, Brian K. Kay

Research output: Contribution to journalReview articlepeer-review

Abstract

Bacteriophage M13 virions are very stable nanoparticles that can be modified by chemical and genetic methods. The capsid proteins can be functionalized in a variety of chemical reactions without loss of particle integrity. In addition, Genetic Code Expansion (GCE) permits the introduction of non-canonical amino acids (ncAAs) into displayed peptides and proteins. The incorporation of ncAAs into phage libraries has led to the discovery of high-affinity binders with low nanomolar dissociation constant (KD) values that can potentially serve as inhibitors. This article reviews how bioconjugation and the incorporation of ncAAs during translation have expanded the chemistry of peptides and proteins displayed by M13 virions for a variety of purposes.

Original languageEnglish (US)
Article number961093
JournalFrontiers in Microbiology
Volume13
DOIs
StatePublished - Aug 8 2022

Keywords

  • antibody fragments
  • bioconjugation
  • combinatorial peptide libraries
  • cross-linking
  • cyclization
  • peptide
  • phage-display
  • stop codon suppression

ASJC Scopus subject areas

  • Microbiology
  • Microbiology (medical)

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