Desorption/Ionization Efficiency of Peptides Containing Disulfide Bonds in Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry

• SHIGERI Yasushi

  Health Research Institute, National Institute of Advanced Industrial Science and Technology

• INAZUMI Satoshi

  Department of Chemistry and Materials Engineering, Kansai University

• HAGIHARA Yoshihisa

  Health Research Institute, National Institute of Advanced Industrial Science and Technology

• YASUDA Akikazu

  Health Research Institute, National Institute of Advanced Industrial Science and Technology

• KAWASAKI Hideya

  Department of Chemistry and Materials Engineering, Kansai University

• ARAKAWA Ryuichi

  Department of Chemistry and Materials Engineering, Kansai University

• NAKATA Makoto

  SAITO Research Center, Peptide Institute, Inc.

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, [Arg⁸]-vasopressin, [Arg⁸]-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.

Journal

• Analytical Sciences

  Analytical Sciences 28 (3), 295-295, 2012

  The Japan Society for Analytical Chemistry

Keywords

• Analytical Chemistry

Details

• CRID: 1390001204259207936
• NII Article ID: 130004442128
• NII Article ID: 10030447339
• NII Book ID: AA10500785
• DOI: 10.2116/analsci.28.295
• COI: 1:STN:280:DC%2BC38vpvVKgug%3D%3D
• ISSN: 13482246
• ISSN: 09106340
• NDL BIB ID: 023495817
• PubMed: 22451371
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I023495817
• Web Site: https://link.springer.com/content/pdf/10.2116/analsci.28.295.pdf
• Web Site: https://link.springer.com/article/10.2116/analsci.28.295/fulltext.html
• Web Site: https://www.jstage.jst.go.jp/article/analsci/28/3/28_3_295/_pdf
• Text Lang: en
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • PubMed
  • CiNii Articles
  • KAKEN
• Abstract License Flag: Disallowed