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	Binding of copper (II) ion to an Alzheimer's tau peptide as revealed by MALDI-TOF MS, CD, and NMR
	Ma, OF ; Li, YM ; Du, JT ; Kanazawa, K ; Nemoto, T ; Nakanishi, H ; Zhao, YF
	2010-05-06 ; 2010-05-06
关键词	copper binding matrix assisted laser desorption/ionization time of flight mass spectrometry (MALDI-TOF MS) NAIR spectroscopy R3 peptide tau protein PAIRED HELICAL FILAMENTS AMYLOID PRECURSOR PROTEIN CIRCULAR-DICHROISM PRION PROTEIN BETA-PEPTIDE IN-VITRO FRONTOTEMPORAL DEMENTIA ALPHA-HELIX AMINO ACIDS HUMAN-BRAIN Biochemistry & Molecular Biology Biophysics
中文摘要	The tau protein plays an important role in some neurodegenerative diseases including Alzheimer's disease (AD). Neurofibrillary tangles (NFTs), a biological marker for AD, are aggregates of bundles of paired helical filaments (PHFs). In general, the a-sheet structure favors abet-rant protein aggregates. However, some reports have shown that the a-helix structure is capable of triggering the formation of abet-rant tau protein aggregates and PHFs have a high a-helix content. In addition, the third repeat fragment in the four-repeat microtubule-binding domain of the tau protein (residues 306-336: VQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQ, according to the longest tau protein) adopts a helical structure in trifluoroethanol (TFE) and may be a self-assembly model in the tau protein. In the human brain, there is a very small quantity of copper, which performs an important function. In our study, by means of matrix assisted laser desorption/ionization time of flight mass spectrometry (MALDI-TOF MS), circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy, the binding properties of copper (II) ion to the R3 peptide derived from the third repeat fragment (residues 318-335: VTSKCGSLGNIHHKPGGG) have been investigated. The results show that copper ions bind to the R3 peptide. CD spectra, ultraviolet (UV)-visible absorption spectra, and MALDI-TOF MS show pH dependence and stoichiometry of Cu2+ binding. Furthermore, CD spectra and NMR spectroscopy elucidate the copper binding sites located in the R3 peptide. Finally, CD spectra reveal that the R3 peptide adopts a mixture structure of random structures, a-helices, and P-turns in aqueous solutions at physiological pH. At pH 7.5, the addition of 0.25 mot eq of Cu2+ induces the conformational change from the mixture mentioned above to a monomeric helical structure, and a P-sheet structure forms in the presence of 1 mol eq of Cu2+. As a-helix and P-sheet structures are responsible for the formation of PHFs, it is hypothesized that Cu2+ is an inducer of self-assembly of the R3 peptide and makes the R3 peptide form a structure like PHF. Hence, it is postulated that Cu2+ plays an important role in the aggregation of the R3 peptide and tau protein and that copper (II) binding may be another possible involvement in AD. (c) 2005 Wiley Periodicals, Inc.
语种	英语 ; 英语
出版者	JOHN WILEY & SONS INC ; HOBOKEN ; 111 RIVER ST, HOBOKEN, NJ 07030 USA
内容类型	期刊论文
源URL	[http://hdl.handle.net/123456789/13550]
专题	清华大学
推荐引用方式 GB/T 7714	Ma, OF,Li, YM,Du, JT,et al. Binding of copper (II) ion to an Alzheimer's tau peptide as revealed by MALDI-TOF MS, CD, and NMR[J],2010, 2010.
APA	Ma, OF.,Li, YM.,Du, JT.,Kanazawa, K.,Nemoto, T.,...&Zhao, YF.(2010).Binding of copper (II) ion to an Alzheimer's tau peptide as revealed by MALDI-TOF MS, CD, and NMR..
MLA	Ma, OF,et al."Binding of copper (II) ion to an Alzheimer's tau peptide as revealed by MALDI-TOF MS, CD, and NMR".(2010).

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