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A Model of Amyloid's Role in Disease Based on Fibril Fracture by Damien Hall; Herman Edskes is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Although the correlative evidence relating the presence of amyloid fibrils and certain disease states (e.g. Alzheimer's disease and Type 2 Diabetes) is overwhelming, a direct causative role for amyloid has proved harder to establish. Current thinking links a narrow region of the aggregate protein size distribution, the so called 'early aggregate' domain to cellular toxicity. A troubling feature of this theory however is that the nucleated reaction mechanism by which amyloid formation is believed to occur results in a very low number concentration of early aggregates which are rapidly extended to form amyloid fibrils. This situation means that the concentration of early aggregates is very low at the time when they are supposedly at their most toxic. Here we adopt a novel explicit simulation strategy to examine a kinetic regime involving nucleated growth combined with fibril fragmentation under which this situation can be reversed so as to produce a high number concentration of small on-pathway toxic aggregates. Dependent upon the rate of fragmentation, the time scale for generation of toxic early aggregates may be coupled, uncoupled or disassociated from the time scale for the appea

Who reads A Model of Amyloid's Role in Disease Based on Fibril Fracture?

Author

Damien Hall; Herman Edskes

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 0301-4622)

Published

2009

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)