Difference in Fibril Core Stability between Two Tau Four-Repeat Domain Proteins: A Hydrogen–Deuterium Exchange Coupled to Mass Spectrometry Study
Biochemistry2013Vol. 52(49), pp. 8787–8789
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Abstract
One of the signatures of Alzheimer's disease and tauopathies is fibrillization of the microtubule-associated protein tau. The purpose of this study was to compare the high-resolution structure of fibrils formed by two different tau four-repeat domain constructs, tau4RD and tauK18, using hydrogen-deuterium exchange coupled to mass spectrometry as a tool. While the two fibrils are found to be constructed on similar structural principles, the tauK18 fibril has a slightly more stable core. This difference in fibril core stability appears to be reflective of the mechanistic differences in the aggregation pathways of the two proteins.
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