Abstract

Oral Sessions

Day 3, May 17（Fri.）　14:45-15:05　Room C (101)

3C-O2-1445　　PDF

Affinity of Protein-Protein and Protein-Ligand Interactions Analyzed by Native Mass Spectrometry

(¹Osaka Univ., ²ExCELLS)
^oSusumu Uchiyama^1,2

We have been studying on protein-protein interactions and protein-ligand interactions as well as supramolecules composed of designed synthetic molecules by native mass spectrometry (native MS) and other biophysical methods such as analytical ultracentrifugation and isothermal titration calorimetry. In addition to stoichiometry of the interactions, estimations of thermodynamic and kinetic parameters are expected for the assessment of stability and dynamics of formed complexes. One approach to derive the quantity of each species based on native MS is analyzing the relative signal intensities of the free and bound states. In the presentation, examples of estimating quantitative interaction parameters in our researches and reports from other groups will be introduced followed by discussion about the pros and cons of native mass spectrometry.