Premium
Photoaffinity Probes for Identification of Carbohydrate‐Binding Proteins
Author(s) -
Sakurai Kaori
Publication year - 2015
Publication title -
asian journal of organic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.846
H-Index - 44
eISSN - 2193-5815
pISSN - 2193-5807
DOI - 10.1002/ajoc.201402209
Subject(s) - chemistry , photoaffinity labeling , glycan , carbohydrate , biotinylation , biochemistry , monosaccharide , protein–protein interaction , carbohydrate responsive element binding protein , computational biology , binding site , glycoprotein , biology , transcription factor , gene
Carbohydrate‐protein interactions mediate cellular signals, which are crucial in a diverse array of biological and pathological processes. Despite their importance, many carbohydrate‐protein interactions remain unknown due to inherent difficulties in studying them. With the aim to provide the first step in elucidating the biological roles of carbohydrates, photoaffinity labeling has been used as a promising chemical strategy for the detection and identification of carbohydrate‐binding proteins in their native environment. Recent efforts in the design of carbohydrate‐based photoaffinity probes include the use of selective photoreactive groups, development of biotinylated photoreactive groups and linkers, multivalent carbohydrate ligands, affinity‐based protein profiling probes, and photoreactive monosaccharide precursors for metabolic glycan labeling. These methods offer new tools to address challenges associated in capturing the often elusive carbohydrate‐protein interactions.