Preliminary mechanistic information on disulfide-bond formation and the role of hydrogen bonds by nanoelectrospray mass spectrometry

✍ Scribed by Honghai Jiang; Minfeng Li; Marie A. Moy; Bing Gong; Troy D. Wood

• Book ID: 102376151
• Publisher: John Wiley and Sons
• Year: 2008
• Tongue: English
• Weight: 238 KB
• Volume: 43
• Category: Article
• ISSN: 1076-5174
• DOI: 10.1002/jms.1366

✦ Synopsis

Abstract

The formation of disulfide‐bonds is vital for the proper folding of most secreted proteins and the stabilization of the final protein structure, including many of medical importance. The determination of disulfide‐bonds is an important aspect of gaining a comprehensive understanding of the chemical structure of a protein. A long‐term goal of ours is to examine the mechanism of disulfide‐bond formation in aqueous solution and the potential role hydrogen bonds play in this process. Here, we report preliminary results from a method that utilizes the oxidizing power of iodine to generate disulfide bonds from synthesized model compounds, which is followed by nanoelectrospray ionization (nanoESI)‐ mass spectrometry (MS). By continuously monitoring the reaction mixture during disulfide formation, this nanoESI approach provides insight on the sequence of intermediate species formed, and how hydrogen‐bonding donor/acceptor pairs may promote disulfide bond formation. Copyright © 2008 John Wiley & Sons, Ltd.