CORRELATION AMONG SECONDARY STRUCTURE, AMYLOID PRECURSOR PROTEIN ACCUMULATION, AND NEUROTOXICITY OF AMYLOID BETA(25-35) PEPTIDE AS ANALYZED BY SINGLE ALANINE SUBSTITUTION

被引:45
作者
SATO, K [1 ]
WAKAMIYA, A [1 ]
MAEDA, T [1 ]
NOGUCHI, K [1 ]
TAKASHIMA, A [1 ]
IMAHORI, K [1 ]
机构
[1] KITASATO UNIV,DEPT PHYS,SAGAMIHARA,KANAGAWA 228,JAPAN
关键词
AGGREGATION; AMYLOID BETA PROTEIN; BETA-SHEET CONFORMATION; HYDROPHOBICITY; NEUROTOXICITY;
D O I
10.1093/oxfordjournals.jbchem.a124994
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Structure-neurotoxicity relationships of amyloid beta(25-35) peptide were studied by replacing each amino acid with Ala, In contrast to the general tendency in hydrophobicity-toxicity relationships, replacement of Asn(27) yielded a more hydrophobic but less toxic analog and that of Met(35) gave a less hydrophobic but more toxic one, Sedimentation profiles and CD spectra indicated that peptide aggregation via intermolecular beta-sheet formation is essential for the neurotoxicity of amyloid beta(25-35) peptide, The correlation between neurotoxicity and amyloid precursor protein accumulation suggested that the latter is one of the pathways of the neuronal death caused by amyloid beta protein.
引用
收藏
页码:1108 / 1111
页数:4
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