Mutation of M13 Bacteriophage Major Coat Protein for Increased Conjugation to Exogenous Compounds.

Matthew Tridgett, James R. Lloyd, Jack Kennefick, Charles Moore-Kelly, Timothy Dafforn

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)
213 Downloads (Pure)

Abstract

Over the past ten years there has been increasing interest in the conjugation of exogenous compounds to the surface of the M13 bacteriophage. M13 offers a convenient scaffold for the development of nanoassemblies with useful functions, such as highly specific drug delivery and pathogen detection. However, the progress of these technologies has been hindered by the limited efficiency of conjugation to the bacteriophage. Here we generate a mutant version of M13 with an additional lysine residue expressed on the outer surface of the M13 major coat protein, pVIII. We show that this mutation is accommodated by the bacteriophage and that up to an additional 520 exogenous groups can be attached to the bacteriophage surface via amine-directed conjugation. These results could aid the development of high payload drug delivery nanoassemblies and pathogen detection systems with increased sensitivity
Original languageEnglish
Pages (from-to)1872-1875
Number of pages4
JournalBioconjugate Chemistry
Volume29
Issue number6
Early online date25 May 2018
DOIs
Publication statusPublished - 20 Jun 2018

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