Soluble multimeric Alzheimer β(1-40) pre-amyloid complexes in dilute solution

Harry Levine

doi:10.1016/0197-4580(95)00052-G

Soluble multimeric Alzheimer β(1-40) pre-amyloid complexes in dilute solution

Harry Levine

Molecular and Cellular Biochemistry

Research output: Contribution to journal › Article › peer-review

97 Scopus citations

Abstract

Aqueous solutions of β(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 β-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 {left and right arrow, wavy} multimer equilibrium may partly explain the divergence of biological consequences with respect to neurotoxicity.

Original language	English
Pages (from-to)	755-764
Number of pages	10
Journal	Neurobiology of Aging
Volume	16
Issue number	5
DOIs	https://doi.org/10.1016/0197-4580(95)00052-G
State	Published - 1995

Keywords

Borohydride reduction SDS-PAGE
Crosslinking
Fibril formation model
Glutaraldehyde
Multimers
Synthetic peptide
pH dependence

ASJC Scopus subject areas

General Neuroscience
Aging
Clinical Neurology
Developmental Biology
Geriatrics and Gerontology

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10.1016/0197-4580(95)00052-G

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title = "Soluble multimeric Alzheimer β(1-40) pre-amyloid complexes in dilute solution",

abstract = "Aqueous solutions of β(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 β-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 {left and right arrow, wavy} multimer equilibrium may partly explain the divergence of biological consequences with respect to neurotoxicity.",

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N2 - Aqueous solutions of β(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 β-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 {left and right arrow, wavy} multimer equilibrium may partly explain the divergence of biological consequences with respect to neurotoxicity.

AB - Aqueous solutions of β(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 β-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 {left and right arrow, wavy} multimer equilibrium may partly explain the divergence of biological consequences with respect to neurotoxicity.

KW - Borohydride reduction SDS-PAGE

KW - Crosslinking

KW - Fibril formation model

KW - Glutaraldehyde

KW - Multimers

KW - Synthetic peptide

KW - pH dependence

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JO - Neurobiology of Aging

JF - Neurobiology of Aging

IS - 5

ER -

Soluble multimeric Alzheimer β(1-40) pre-amyloid complexes in dilute solution

Abstract

Keywords

ASJC Scopus subject areas

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