Mutation of M13 Bacteriophage Major Coat Protein for Increased Conjugation to Exogenous Compounds.
Bioconjug Chem
; 29(6): 1872-1875, 2018 06 20.
Article
in En
| MEDLINE
| ID: mdl-29800521
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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Bacteriophage M13
/
Capsid Proteins
/
Amines
Language:
En
Journal:
Bioconjug Chem
Journal subject:
BIOQUIMICA
Year:
2018
Document type:
Article
Affiliation country: