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Electrospray ionization-induced protein unfolding Open Access


Author or creator
Lin, Hong
Kitova, Elena N.
Johnson, M. A., Eugenio, Luiz
Ng, Kenneth K.
Klassen, John S.
Additional contributors
Electrospray ionization
Charging mechanism
Protein unfolding
Type of item
Journal Article (Published)
Electrospray ionization mass spectrometry (ESI-MS) measurements were performed under a variety of solution conditions on a highly acidic sub-fragment (B3C) of the C-terminal carbohydrate-binding repeat region of Clostridium difficile toxin B, and two mutants (B4A and B4B) containing fewer acidic residues. ESI-MS measurements performed in negative ion mode on aqueous ammonium acetate solutions of B3C at low ionic strength (I  10 mM. The results of ESI-MS measurements performed on B3C in a series of solutions with high I at pH 5 to 9 rule out the possibility that the structural changes are related to ESI-induced changes in pH. It is proposed that unfolding of B3C, observed in negative mode for solutions with low I, occurs during the ESI process and arises due to Coulombic repulsion between the negatively charged residues and liquid/droplet surface charge. ESI-MS measurements performed in negative ion mode on B4A and B4B also reveal a shift to higher charge states at low I but the magnitude of the changes are smaller than observed for B3C.
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© 2012 Lin, H., Kitova, E. N., Johnson, M. A., Eugenio, L., Ng, K. K., & Klassen, J. S. This version of this article is open access and can be downloaded and shared. The original author(s) and source must be cited.

Citation for previous publication
Lin, H., Kitova, E. N., Johnson, M. A., Eugenio, L., Ng, K. K., & Klassen, J. S. (2012). Electrospray ionization-induced protein unfolding. Journal of the American Society for Mass Spectrometry, 23(12), 2122-2131.


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