Oral Presentation HUPO 2019 - 18th Human Proteome Organization World Congress

Development of gold nanoparticle-based multivalent photoaffinity probes toward exploration of carbohydrate-protein interaction (#65)

Kaori Sakurai 1
  1. Tokyo University of Agriculture and Technology, Koganei-shi, TOKYO, Japan

Carbohydrate-protein interactions mediate cellular signals, which are crucial in a diverse array of biological and pathological processes.  Despite their importance, many of carbohydrate-protein interactions remain unknown due to inherent difficulties in studying them.  While chemical methods involving affinity probes and affinity matrixes offer most direct and rapid ways to explore cellular targets, their utility is often limited particularly in the case with carbohydrate binding proteins with low affinity.  With the aim to provide the first step in elucidating the biological roles of carbohydrates, photoaffinity labeling has been employed as a promising chemical strategy for the detection and the identification of carbohydrate-binding proteins in their native environment.  In this presentation, I will introduce a new approach, which employs multivalent photoaffinity probes based on gold-nanoparticles for streamlined analysis of carbohydrate-protein interactions.  Gold nanoparticles are attractive scaffolds for chemical probes based on several advantages.  The probe design can be optimized rapidly owing to facile and modular functionalization of gold nanoparticles with various composition of a ligand and a photoreactive group.  Multivalent display of ligands and photoreactive groups promotes increased protein binding affinity as well as enhanced protein reactivity.  Proteins can be easily enriched on gold nanoparticle probes by centrifugal separation from the protein mixture.  Therefore, gold nanoparticles can serve both as a scaffold for affinity probes in solution and as an affinity matrix separable from solution.  Since preparation of chemical probes and their application to target identification studies are often laborious, multistep processes, our approach should be useful for expediting the identification and analysis of target proteins.