Enhanced correction methods for hydrogen exchange-mass spectrometric studies of amyloid fibrils |
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Authors: | Kheterpal Indu Wetzel Ronald Cook Kelsey D |
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Institution: | Graduate School of Medicine, University of Tennessee Medical Center, University of Tennessee, Knoxville, Tennessee 37996-1600, USA. |
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Abstract: | We describe methods for minimization of and correction for artifactual forward and backward exchange occurring during hydrogen exchange-mass spectrometric (HX-MS) studies of amyloid fibrils of the Abeta(1-40) peptide. The quality of the corrected data obtained using published and new correction algorithms is evaluated quantitatively. Using the new correction methods, we have determined that 20.1 +/- 1.4 of the 39 backbone amide hydrogens in Abeta(1-40) exchange with deuteriums in 100 h when amyloid fibrils of this peptide are suspended in D(2)O. These data reinforce our previous conclusions based on uncorrected data that amyloid fibrils contain a rigid protective core structure that involves only about half of the Abeta backbone amides. The methods developed here should be of general value for HX-MS studies of amyloid fibrils and other protein aggregates. |
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Keywords: | Hydrogen exchange Aβ amyloid electrospray ionization mass spectrometry |
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