演題概要

ポスター発表

第3日　5月13日（水）　　P会場（1008/09）

3P-35　　PDF

サイクリック・トラベリングウェーブ・イオンモビリティ-質量分析法を用いたバソトシン・ノナペプチド・ジアステレオマーの立体配座多様性の測定

(¹Vanderbilt University・ ²ウォーターズ・ ³日本ウォーターズ)
Phillips, Shawn¹・ Zlibut, Emanuel¹・ May, Jody¹・ Mclean, John¹・ Palmer, Martin²・ Cooper-shepherd, Dale²・ Langridge, James²・ ^o押方基二³

Vasotocin nonapeptides are 9-amino acid peptide hormones responsible for fluid regulation (vasopressin family) and promoting social bonding (oxytocin family) and are implicated in a variety of developmental disorders, including autism, depression, and schizophrenia. The mechanism of action involves binding to vascular receptors, and a synthetic analogue, desmopressin, has demonstrated significantly decreased binding affinity through the substitution of the 8th residue, L-arginine, with its enantiomer, D-arginine, suggesting this residue significantly impacts the resulting peptide conformation. Prior ion mobility-mass spectrometry (IM-MS) studies showed direct IM separation of chiral nonapeptides. Here we present results from IM-MS and cyclic traveling wave IM (cIM) that resolve additional conformer populations within these diastereomeric peptides, as well as evidence for interconverting conformers co-existing during IM-MS analyses.

Keywords:
Ion mobility, Diastereomer, peptide hormone, collisional cross section, CCS, HRMS

Novel Aspect:
Multiple conformer populations for lasso peptides revealed by high resolution cyclic IM and tandem IM/IM experiments.