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Bioconjugation of therapeutic proteins and enzymes using the expanded set of genetically encoded amino acids.

Authors
  • Lim, Sung In1
  • Kwon, Inchan1, 2
  • 1 a Department of Chemical Engineering , University of Virginia , Charlottesville , VA , USA and.
  • 2 b School of Materials Science and Engineering, Gwangju Institute of Science and Technology (GIST) , Gwangju , Republic of Korea.
Type
Published Article
Journal
Critical reviews in biotechnology
Publication Date
October 2016
Volume
36
Issue
5
Pages
803–815
Identifiers
DOI: 10.3109/07388551.2015.1048504
PMID: 26036278
Source
Medline
Keywords
License
Unknown

Abstract

The last decade has witnessed striking progress in the development of bioorthogonal reactions that are strictly directed towards intended sites in biomolecules while avoiding interference by a number of physical and chemical factors in biological environment. Efforts to exploit bioorthogonal reactions in protein conjugation have led to the evolution of protein translational machineries and the expansion of genetic codes that systematically incorporate a range of non-natural amino acids containing bioorthogonal groups into recombinant proteins in a site-specific manner. Chemoselective conjugation of proteins has begun to find valuable applications to previously inaccessible problems. In this review, we describe bioorthogonal reactions useful for protein conjugation, and biosynthetic methods that produce proteins amenable to those reactions through an expanded genetic code. We then provide key examples in which novel protein conjugates, generated by the genetic incorporation of a non-natural amino acid and the chemoselective reactions, address unmet needs in protein therapeutics and enzyme engineering.

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