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Atomic Level Investigations of Early Aggregation of Tau43 in Water I. Conformational Propensity of Monomeric Tau43

Authors
Chatterjee, PrathitThi-Diem LeBui, Huong T. D.Cho, Myung KeunHam, Sihyun
Issue Date
Aug-2021
Publisher
WILEY-V C H VERLAG GMBH
Keywords
Alzheimer's disease; Protein aggregation; Tau43 protein; Molecular dynamics simulations; Conformational propensity
Citation
BULLETIN OF THE KOREAN CHEMICAL SOCIETY, v.42, no.8, pp 1134 - 1142
Pages
9
Journal Title
BULLETIN OF THE KOREAN CHEMICAL SOCIETY
Volume
42
Number
8
Start Page
1134
End Page
1142
URI
https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/153056
DOI
10.1002/bkcs.12338
ISSN
0253-2964
1229-5949
Abstract
Recent studies in Alzheimer's disease (AD) investigated the precise mechanisms responsible for neurofibrillary tangles (NFT) and senile plaques formation. NFTs, the aggregated Tau protein isoforms, are one of the primary factors behind AD. The corresponding smallest variant Tau43, as paired helical filaments (PHFs), self-assemble into pathological diseased aggregates. However, the molecular details in rationalizing the aggregation propensity of Tau43 remain elusive. Herein, using molecular dynamics simulations on aqueous Tau43, we identify the molecular factors responsible for early behavior of Tau43 aggregation propensity in water. The variant is intrinsically unstructured yet compact in nature, in agreement with previous studies. The PHF6 ((11)VQIVYK(16)) segment is relatively less fluctuating, yet most extended and hydrophobic, thereby shielded from aqueous environment by intermolecular polar interactions between terminal residues. We also compared structural propensities of Tau43 and oppositely charged A beta 42 peptide, providing a comparative understanding of early AD pathway, leading to corresponding drug designing avenues.
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