Desorption/ionization efficiency of peptides containing disulfide bonds in matrix-assisted laser desorption/ionization mass spectrometry |
| |
Authors: | Shigeri Yasushi Inazumi Satoshi Hagihara Yoshihisa Yasuda Akikazu Kawasaki Hideya Arakawa Ryuichi Nakata Makoto |
| |
Institution: | Health Research Institute, National Institute of Advanced Industrial Science and Technology, Ikeda, Osaka, Japan. yasushi.shigeri@aist.go.jp |
| |
Abstract: | In order to elucidate the role of desorption/ionization efficiency of peptides in MALDI-MS, we focused on peptides with disulfide bonds, which form a rigid tertiary structure. We synthesized seven sets of peptides with one disulfide bond (oxytocin, somatostatin, Arg(8)]-vasopressin, Arg(8)]-vasotocin, cortistatin, melanin-concentrating hormone, urotensin II-related peptide) and five sets of peptides with two disulfide bonds (tertiapin, α-conotoxin GI, α-conotoxin ImI, α-conotoxin MI and α-conotoxin SI). Each peptide set consisted of three peptides: the oxidized form (S-S type), the reduced form (SH type), and an internal standard peptide in which all cysteine residues were substituted with alanine residues. In the case of urotensin II-related peptide, tertiapin, α-conotoxin ImI and α-conotoxin MI, the reduced form showed higher desorption/ionization efficiency than the oxidized form. In contrast, the other peptides revealed higher desorption/ionization efficiency in the oxidized form relative to the reduced form. These results imply that a rigid structure of peptides formed by disulfide bonds does not correlate with desorption/ionization efficiency in MALDI-MS. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|