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

Poster Presentations

Day 1, June 22（Wed.）　　Room P (501, 502 and 503)

1P-06　　PDF

Fragmentation of peptides by MALDI-ISD using 4-hydroxychalcone as a matrix

(1Hiroshima Univ., 2Shimadzu)
oManaho Yamaguchi1, Yuko Fukuyama2, Koichi Tanaka2, Shunsuke Izumi1

Matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) has been known as a soft ionization method that is less fragmentation of analytes. Many matrices contain phenolic hydroxyl groups that ionize the analyte by laser energy and simultaneously contain carboxy groups, but their role is still unclear. In this study, MALDI-ISD experiment was performed for angiotensin II by MALDI-MS instrument with laser at 337 nm or 355 nm, using 4-hydroxychalcone as a matrix. As a result, a-ions were detected at 355 nm, although no ISD fragments were detected at 337 nm. This formation of a-ion indicates that at 355 nm the radical source in the matrix pull out the amide hydrogen of the peptide backbone. Therefore, this result of a-ion preferential formation is suggested to be caused by carbonyl oxygen radical in 4-hydroxychalcone structure.