The protein-surfactant stoichiometry governs the conformational switching and amyloid nucleation kinetics of tau K18.

European Biophysics Journal : EBJ
Jaspreet KaurMily Bhattacharya

Abstract

Amyloids are pathological hallmarks of a number of debilitating neurodegenerative diseases. Understanding the molecular mechanism of protein amyloid assembly with an emphasis on structural characterization of early, key prefibrillar species is important for targeted drug design and clinical interventions. Tau is an intrinsically disordered, microtubule-binding protein which is also implicated in various neurodegenerative disorders such as frontotemporal dementia, Down's syndrome, Alzheimer's disease, etc. Earlier reports have demonstrated that tau aggregation in vitro is triggered by anionic inducers, presumably due to charge compensation which facilitates intermolecular association between the tau polypeptide chains. However, the molecular mechanism of tau amyloid aggregation, involving the structural characterization of amyloidogenic intermediates formed especially during early key steps, remains elusive. In this work, we have employed a spectroscopic toolbox to elucidate the mechanism of anionic surfactant-induced disorder-to-order amyloid transition of a tau segment. This study revealed that the amyloid assembly is mediated via binding-induced conformational switching into an early partially helical amyloid-competent interm...Continue Reading

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Citations

Sep 20, 2021·Journal of Molecular Biology·Sreemantee SenJayant B Udgaonkar

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Methods Mentioned

BETA
atomic force microscopy
AFM
circular dichroism
fluorescence spectroscopy
cross-linking assay
dynamic light scattering

Software Mentioned

WSxM
NanoDrive
OriginLab Pro

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