Issue 4, 2011
From the journal:

Molecular BioSystems

Zinc-induced dimerization of the amyloid-β metal-binding domain 1–16 is mediated by residues 11–14†

Sergey A. Kozin,*ab   Yuri V. Mezentsev,b   Alexandra A. Kulikova,a   Maria I. Indeykina,ac   Andrey V. Golovin,d   Alexis S. Ivanov,b   Philipp O. Tsvetkovab  and  Alexander A. Makarov*a  

* Corresponding authors

a Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov street 32, 119991 Moscow, Russia
E-mail: aamakarov@eimb.ru, kozinsa@gmail.com

b Orekhovich Institute of Biomedical Chemistry, Russian Academy of Medical Sciences, Pogodinskaya street 10, 119832 Moscow, Russia

c Emanuel Institute of Biochemical Physics, Kosygina street 4, 119334 Moscow, Russia

d Bioengineering and Bioinformatics Department, M. V. Lomonosov Moscow State University, Leninskie Gory 1, 119992 Moscow, Russia

Abstract

Analysis of complex formation between amyloid-β fragments using surface plasmon resonance biosensing and electrospray mass spectrometry reveals that region 11–14 mediates zinc-induced dimerization of amyloid-β and may serve as a potential drug target for preventing development and progression of Alzheimer's disease.

Graphical abstract: Zinc-induced dimerization of the amyloid-β metal-binding domain 1–16 is mediated by residues 11–14

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Article information

DOI
https://doi.org/10.1039/C0MB00334D
Article type
Communication
Submitted
16 Dec 2010
Accepted
01 Feb 2011
First published
25 Feb 2011

Mol. BioSyst., 2011,7, 1053-1055

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Zinc-induced dimerization of the amyloid-β metal-binding domain 1–16 is mediated by residues 11–14

S. A. Kozin, Y. V. Mezentsev, A. A. Kulikova, M. I. Indeykina, A. V. Golovin, A. S. Ivanov, P. O. Tsvetkov and A. A. Makarov, Mol. BioSyst., 2011, 7, 1053 DOI: 10.1039/C0MB00334D

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