Photoaffinity Probes for the Identification of Sequence-Specific Glycosaminoglycan-Binding Proteins.

ABSTRACT: Glycosaminoglycan (GAG)-protein interactions mediate critical physiological and pathological processes, such as neuronal plasticity, development, and viral invasion. However, mapping GAG-protein interaction networks is challenging as these interactions often require specific GAG sulfation patterns and involve transmembrane receptors or extracellular matrix-associated proteins. Here, we report the first GAG polysaccharide-based photoaffinity probes for the system-wide identification of GAG-binding proteins in living cells. A general platform for the modular, efficient assembly of various chondroitin sulfate (CS)-based photoaffinity probes was developed. Systematic evaluations led to benzophenone-containing probes that efficiently and selectively captured known CS-E-binding proteins in vitro

SUBMITTER: Joffrin AM 

PROVIDER: S-EPMC7641097 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature