Preliminary mechanistic information on disulfide-bond formation and the role of hydrogen bonds by nanoelectrospray mass spectrometry.
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.
Jiang
Honghai
H
Department of Chemistry, University at Buffalo, The State University of New York, Buffalo, NY 14260, USA.
Li
Minfeng
M
Moy
Marie A
MA
Gong
Bing
B
Wood
Troy D
TD
D003198:Computer Simulation; D004220:Disulfides / Q000737:chemistry*; D006860:Hydrogen Bonding; D008832:Microchemistry / Q000379:methods*; D008956:Models, Chemical; D036103:Nanotechnology / Q000379:methods*; D010865:Pilot Projects; D021241:Spectrometry, Mass, Electrospray Ionization / Q000379:methods*
D004220:Disulfides