Minimal Zn2+ binding site of amyloid-β

Biophysical Journal

Volumn 99, Issue 10, 2010, Pages

  Tsvetkov, Philipp O ^a,b   Kulikova, Alexandra A ^a   Golovin, Andrey V ^a,c   Tkachev, Yaroslav V ^a   Archakov, Alexander I ^b   Kozin, Sergey A ^a,b   Makarov, Alexander A ^a  

^a ENGELHARDT INSTITUTE OF MOLECULAR BIOLOGY   (Russian Federation)

^b INSTITUTE OF BIOMEDICAL CHEMISTRY   (Russian Federation)

^c MOSCOW STATE UNIVERSITY   (Russian Federation)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 78649288610     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.09.015     Document Type: Article

References (15)

1. Goedert, M., and M. G. Spillantini. 2006. A century of Alzheimer's disease. Science. 314:777-781.
2. Bush, A. I. 2003. The metallobiology of Alzheimer's disease. Trends Neurosci. 26:207-214.
3. Cuajungco,M.P., and K.Y. Faget. 2003. Zinc takes the center stage: its paradoxical role in Alzheimer's disease. Brain Res. Brain Res. Rev. 41:44-56.
4. Maynard, C. J., A. I. Bush,., Q. X. Li. 2005. Metals and amyloid-b in Alzheimer's disease. Int. J. Exp. Pathol. 86:147-159.
5. Tsvetkov, P. O., I. A. Popov,., S. A. Kozin. 2008. Isomerization of the Asp7 residue results in zinc-induced oligomerization of Alzheimer's disease amyloid β (1-16) peptide. ChemBioChem. 9:1564-1567.
6. Faller, P., and C. Hureau. 2009. Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-b peptide. Dalton Trans. 1080-1094.
7. Kozin, S. A., S. Zirah,., P. Debey. 2001. Zinc binding to Alzheimer's Ab (1-16) peptide results in stable soluble complex. Biochem. Biophys. Res. Commun. 285:959-964.
8. Zirah, S., S. A. Kozin, ., S. Rebuffat. 2006. Structural changes of region 1-16 of the Alzheimer disease amyloid β -peptide upon zinc binding and in vitro aging. J. Biol. Chem. 281:2151-2161.
9. Damante, C.A.,K.Osz,., I. Sovago. 2009.Metal loading capacity ofAb N-terminus: a combined potentiometric and spectroscopic study of zinc (II) complexes with Ab (1-16), its short or mutated peptide fragments and its polyethylene glycolated analogue. Inorg. Chem. 48:10405-10415.
10. Danielsson, J., R. Pierattelli, ., A. Graslund. 2007. High-resolution NMR studies of the zinc-binding site of the Alzheimer's amyloid β -peptide. FEBS J. 274:46-59.
11. Gaggelli, E., A. Janicka-Klos, ., E. Wieczerzak. 2008. NMR studies of the Zn2+ interactions with rat and human b-amyloid (1-28) peptides in water-micelle environment. J. Phys. Chem. B. 112:100-109.
12. Toropygin, I. Y., E. V. Kugaevskaya, ., S. A. Kozin. 2008. The N-domain of angiotensin-converting enzyme specifically hydrolyzes the Arg5-His6 bond of Alzheimer's Ab -(1-16) peptide and its isoAsp7 analogue with different efficiency as evidenced by quantitative matrixassisted laser desorption/ionization time-of-flight mass spectrometry. Rapid Commun. Mass Spectrom. 22:231-239.
13. Talmard, C., L. Guilloreau, ., P. Faller. 2007. Amyloid-b peptide forms monomeric complexes with Cu(II) and Zn(II) prior to aggregation. ChemBioChem. 8:163-165.
14. Miller, Y., B. Ma, and R. Nussinov. 2010. Zinc ions promote Alzheimer Ab aggregation via population shift of polymorphic states. Proc. Natl. Acad. Sci. USA. 107:9490-9495.
15. Furlan, S., and G. La Penna. 2009. Modeling of the Zn2+ binding in the 1-16 region of the amyloid β peptide involved in Alzheimer's disease. Phys. Chem. Chem. Phys. 11:6468-6481.