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Tytuł pozycji:

A theoretical study of polymorphism in VQIVYK fibrils.

Tytuł:
A theoretical study of polymorphism in VQIVYK fibrils.
Autorzy:
Yang J; Department of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio.
Agnihotri MV; Interdisciplinary Biophysics Graduate Program, The Ohio State University, Columbus, Ohio.
Huseby CJ; Interdisciplinary Biophysics Graduate Program, The Ohio State University, Columbus, Ohio.
Kuret J; Interdisciplinary Biophysics Graduate Program, The Ohio State University, Columbus, Ohio; Department of Biological Chemistry and Pharmacology, The Ohio State University, Columbus, Ohio. Electronic address: .
Singer SJ; Department of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio; Interdisciplinary Biophysics Graduate Program, The Ohio State University, Columbus, Ohio. Electronic address: .
Źródło:
Biophysical journal [Biophys J] 2021 Apr 20; Vol. 120 (8), pp. 1396-1416. Date of Electronic Publication: 2021 Feb 09.
Typ publikacji:
Journal Article; Research Support, N.I.H., Extramural
Język:
English
Imprint Name(s):
Publication: Cambridge, MA : Cell Press
Original Publication: New York, Published by Rockefeller University Press [etc.] for the Biophysical Society.
MeSH Terms:
Amyloid*
tau Proteins*/genetics
tau Proteins*/metabolism
Cryoelectron Microscopy ; Humans ; Hydrophobic and Hydrophilic Interactions ; Models, Theoretical ; Protein Conformation, beta-Strand
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Grant Information:
RF1 AG054018 United States AG NIA NIH HHS
Substance Nomenclature:
0 (Amyloid)
0 (tau Proteins)
Entry Date(s):
Date Created: 20210211 Date Completed: 20210531 Latest Revision: 20220421
Update Code:
20240104
PubMed Central ID:
PMC8105716
DOI:
10.1016/j.bpj.2021.01.032
PMID:
33571490
Czasopismo naukowe
The VQIVYK fragment from the Tau protein, also known as PHF6, is essential for aggregation of Tau into neurofibrillary lesions associated with neurodegenerative diseases. VQIVYK itself forms amyloid fibrils composed of paired β-sheets. Therefore, the full Tau protein and VQIVYK fibrils have been intensively investigated. A central issue in these studies is polymorphism, the ability of a protein to fold into more than one structure. Using all-atom molecular simulations, we generate five stable polymorphs of VQIVYK fibrils, establish their relative free energy with umbrella sampling methods, and identify the side chain interactions that provide stability. The two most stable polymorphs, which have nearly equal free energy, are formed by interdigitation of the mostly hydrophobic VIY "face" sides of the β-sheets. Another stable polymorph is formed by interdigitation of the QVK "back" sides. When we turn to examine structures from cryo-electron microscopy experiments on Tau filaments taken from diseased patients or generated in vitro, we find that the pattern of side chain interactions found in the two most stable face-to-face as well as the back-to-back polymorphs are recapitulated in amyloid structures of the full protein. Thus, our studies suggest that the interactions stabilizing PHF6 fibrils explain the amyloidogenicity of the VQIVYK motif within the full Tau protein and provide justification for the use of VQIVYK fibrils as a test bed for the design of molecules that identify or inhibit amyloid structures.
(Copyright © 2021 Biophysical Society. Published by Elsevier Inc. All rights reserved.)

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