SOLUBLE MULTIMERIC ALZHEIMER BETA(1-40) PRE-AMYLOID COMPLEXES IN DILUTE-SOLUTION
SOLUBLE MULTIMERIC ALZHEIMER BETA(1-40) PRE-AMYLOID COMPLEXES IN DILUTE-SOLUTION
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DOI：
10.1016/0197-4580(95)00052-g
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发表时间：
1995-09-01
影响因子：
4.2
通讯作者：
LEVINE, H
中科院分区：
文献类型：
--
作者：
LEVINE, H
β（1-40）肽的水溶液自发地缔合形成五聚体/六聚体复合物，其可以在用戊二醛和硼氢化物还原处理后通过SDS-PAGE证明。在pH和高肽浓度的淀粉样蛋白生成条件下，这些聚集体可以进一步结合形成具有硫磺素T荧光的β-折叠淀粉样蛋白特征的可沉淀和可过滤结构。在低肽浓度下，这种淀粉样结构的存在表明了一种机制，通过这种机制，淀粉样斑块可以通过合作而不是单体生长来增加额外的物质。单体多聚体平衡的存在可以部分解释神经毒性生物学后果的分歧。
Aqueous solutions of beta(1-40) peptide spontaneously associate to form pentameric/hexameric complexes that can be demonstrated by SDS-PAGE following treatment with glutaraldehyde and borohydride reduction. Under amyloidogenic conditions of pH and high peptide concentration these aggregates can further associate to form sedimentable and filterable structures with beta-sheet amyloid characteristics of Thioflavine T fluorescence. The presence of such preamyloid structures at low peptide concentration suggests a mechanism by which amyloid plaques can accrete additional material by a cooperative rather than monomeric growth. The existence of a monomer multimer equilibrium may partly explain the divergence of biological consequences with respect to neurotoxicity.