Conformational Abs recognizing a generic amyloid fibril epitope.

ONuallain Brian; Wetzel Ronald

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Conformational Abs recognizing a generic amyloid fibril epitope.

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Disease-related amyloid fibrils appear to share a common, but poorly understood, structure. We describe here the generation and preliminary characterization of two conformation-specific mAbs, WO1 and WO2, that bind to the amyloid fibril state of the Alzheimer's peptide A beta(1-40) but not to its soluble, monomeric state. Surprisingly, these Abs also bind to other disease-related amyloid fibrils and amyloid-like aggregates derived from other proteins of unrelated sequence, such as transthyretin, islet amyloid polypeptide, beta(2)-microglobulin, and polyglutamine. At the same time, WO1 and WO2 do not bind to the native protein precursors of these amyloids, nor do they bind to other kinds of protein aggregates. This new class of Abs associated with a fundamental amyloid-folding motif appear to recognize a common conformational epitope with little apparent dependence on amino acid side chain information. These Abs should contribute to the understanding of amyloid structure, assembly, and toxicity and also may benefit the development of diagnostic and therapeutic agents for amyloid diseases.

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《Proceedings of the National Academy of Sciences of the United States of America》 |2002年第3期|1485-1490|共6页
作者
ONuallain Brian; Wetzel Ronald;
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作者单位

Graduate School of Medicine, University of Tennessee Medical Center, 1924 Alcoa Highway, Knoxville, TN 37920, USA.;

itt.edu;

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收录信息美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
原文格式 PDF
正文语种英语
中图分类自然科学总论;
关键词
Amyloid beta-Protein; Epitopes; Peptide Fragments; Amyloid; Antibodies; Monoclonal; 淀粉样β蛋白; 表位; 肽碎片;

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Conformational Abs recognizing a generic amyloid fibril epitope.

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