Issue 34, 2013
From the journal:

Chemical Communications

Molecular insights into the reversible formation of tau protein fibrils†

Yin Luo,a   Paul Dinkel,b   Xiang Yu,c   Martin Margittai,b   Jie Zheng,c   Ruth Nussinov,de   Guanghong Wei*a  and  Buyong Ma*d  

* Corresponding authors

a State Key Laboratory of Surface Physics, Department of Physics, Fudan University, Shanghai, P.R. China
E-mail: ghwei@fudan.edu.cn

b Department of Chemistry & Biochemistry, University of Denver, Denver, Colorado 80208, USA
E-mail: martin.margittai@du.edu

c Department of Chemical & Biomolecular Engineering, The University of Akron, Akron, Ohio 44325, USA
E-mail: zhengj@uakron.edu

d Basic Science Program, SAIC-Frederick, Inc. CCRNP, Frederick National Lab, Frederick, Maryland 21702, USA
E-mail: mabuyong@mail.nih.gov

e Sackler Inst. of Molecular Medicine. Tel Aviv University, Tel Aviv 69978, Israel
E-mail: ruthnu@helix.nih.gov

Abstract

We computationally and experimentally showed that tau protein fibrils can be formed at high temperature. When cooled, the fibrils dissociate back to monomers. Heparin promotes tau fibril formation and prevents its reversion. Our results revealed the physicochemical mechanism of reversible formation of tau fibrils.

Graphical abstract: Molecular insights into the reversible formation of tau protein fibrils

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Article information

DOI
https://doi.org/10.1039/C3CC00241A
Article type
Communication
Submitted
10 Jan 2013
Accepted
14 Mar 2013
First published
15 Mar 2013

Chem. Commun., 2013,49, 3582-3584

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Molecular insights into the reversible formation of tau protein fibrils

Y. Luo, P. Dinkel, X. Yu, M. Margittai, J. Zheng, R. Nussinov, G. Wei and B. Ma, Chem. Commun., 2013, 49, 3582 DOI: 10.1039/C3CC00241A

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