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

Sergey A Kozin; Yuri V Mezentsev; Alexandra A Kulikova; Maria I Indeykina; Andrey V Golovin; Alexis S Ivanov; Philipp O Tsvetkov; Alexander A Makarov

doi:10.1039/c0mb00334d

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

Mol Biosyst. 2011 Apr;7(4):1053-5. doi: 10.1039/c0mb00334d. Epub 2011 Feb 25.

Authors

Sergey A Kozin¹, Yuri V Mezentsev, Alexandra A Kulikova, Maria I Indeykina, Andrey V Golovin, Alexis S Ivanov, Philipp O Tsvetkov, Alexander A Makarov

Affiliation

¹ Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov street 32, 119991 Moscow, Russia.

PMID: 21350790
DOI: 10.1039/c0mb00334d

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Alzheimer Disease / metabolism
Amyloid beta-Peptides / chemistry
Amyloid beta-Peptides / metabolism*
Hydrogen-Ion Concentration
Kinetics
Models, Molecular*
Peptide Fragments / chemistry
Peptide Fragments / metabolism*
Protein Binding
Protein Multimerization*
Temperature
Zinc / chemistry*

Substances

Amyloid beta-Peptides
Peptide Fragments
Zinc