Development and Recent Advances in Lysine and N-Terminal Bioconjugation for Peptides and Proteins

The demand for creation of protein diversity and regulation of protein function through native protein modification and post-translational modification has ignited the development of selective chemical modification methods for peptides and proteins. Chemical bioconjugation offers selective functiona...

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Bibliographic Details
Published in:Molecules (Basel, Switzerland) Switzerland), 2023-01, Vol.28 (3), p.1083
Main Authors: Tantipanjaporn, Ajcharapan, Wong, Man-Kin
Format: Article
Language:English
Subjects:
Amino Acids
Amino groups
Antibody-drug conjugates
Biocompatibility
bioconjugation
Biological products
Biomaterials
Biomedical materials
Carbohydrates
Chemical bonds
Chemical modification
Chemistry
Composition
Health aspects
Lysine
Lysine - chemistry
Materials science
Medical research
Methods
N-terminal modification
N-Terminus
peptide
Peptides
Peptides - chemistry
Post-translation
Post-translational modification
protein
Protein folding
Protein Processing, Post-Translational
Proteins
Proteins - chemistry
Reaction time
Reagents
Residues
Review
Selectivity
site-selectivity
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Summary:The demand for creation of protein diversity and regulation of protein function through native protein modification and post-translational modification has ignited the development of selective chemical modification methods for peptides and proteins. Chemical bioconjugation offers selective functionalization providing bioconjugates with desired properties and functions for diverse applications in chemical biology, medicine, and biomaterials. The amino group existing at the lysine residue and N-terminus of peptides and proteins has been extensively studied in bioconjugation because of its good nucleophilicity and high surface exposure. Herein, we review the development of chemical methods for modification of the amino groups on lysine residue and N-terminus featuring excellent selectivity, mild reaction conditions, short reaction time, high conversion, biocompatibility, and preservation of protein integrity. This review is organized based on the chemoselectivity and site-selectivity of the chemical bioconjugation reagents to the amino acid residues aiming to provide guidance for the selection of appropriate bioconjugation methods.
ISSN:1420-3049
1420-3049
DOI:10.3390/molecules28031083