The Mass Spectrometry society of Japan - The 68th Annual Conference on Mass Spectrometry, Japan
Japanese

Abstract

Table of contents

Timetable

Plenary Lectures

Award Lecture

Oral Sessions (Day1, Day2, Day3)

Poster Presentations (Day1, Day2, Day3)

Panel Discussion

Luncheon Seminars (Day1, Day2, Day3)

Corporate Program

Oral Sessions

Day 1, June 22（Wed.）　17:30-17:50　Room A (Main Hall)

1A-O1-1730　　PDF

Histidine hydrogen-deuterium exchange(His-HDX) mass spectrometry approach for identifying protein-ligand interaction

(1Mitsubishi Tanabe Pharm., 2Case Western Reserve University)
oKohei Tanaka1, Tarou Kishimoto1, Shinko Watanabe1, Kaori Mitsui1, Chieko Okumura1, Kouta Murasaki1, Masaru Miyagi2

It is known that binding of a ligand stabilizes proteins against chemical or heat-induced denaturation. Based on this principle, several mass spectrometry-based proteomic approaches for identifying protein-ligand interactions have been developed, such as SPROX (Stability of Proteins from Rates of Oxidation), DARTS (Drug Affinity Responsive Target Stability), CETSA (Cellular Thermal Shift Assay) and TPP (Thermal Proteome Profiling). Although these methods have shown encouraging results, identifying low abundant and multi-domain proteins is still a challenge. We foresee that histidine hydrogen-deuterium exchange mass spectrometry (His-HDX-MS), which measures the slow HDX of histidine imidazole groups in proteins using mass spectrometry, has the potential to overcome these drawbacks. Here we used His-HDX-MS as a platform to measure heat-induced unfolding of proteins and evaluated the applicability of this platform to identify protein-ligand interactions.