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Crespo2012 - Kinetics of Amyloid Fibril Formation


ABSTRACT: Crespo2012 - Kinetics of Amyloid Fibril Formation This model is described in the article: A generic crystallization-like model that describes the kinetics of amyloid fibril formation. Crespo R, Rocha FA, Damas AM, Martins PM. J. Biol. Chem. 2012 Aug; 287(36): 30585-30594 Abstract: Associated with neurodegenerative disorders such as Alzheimer, Parkinson, or prion diseases, the conversion of soluble proteins into amyloid fibrils remains poorly understood. Extensive "in vitro" measurements of protein aggregation kinetics have been reported, but no consensus mechanism has emerged until now. This contribution aims at overcoming this gap by proposing a theoretically consistent crystallization-like model (CLM) that is able to describe the classic types of amyloid fibrillization kinetics identified in our literature survey. Amyloid conversion represented as a function of time is shown to follow different curve shapes, ranging from sigmoidal to hyperbolic, according to the relative importance of the nucleation and growth steps. Using the CLM, apparently unrelated data are deconvoluted into generic mechanistic information integrating the combined influence of seeding, nucleation, growth, and fibril breakage events. It is notable that this complex assembly of interdependent events is ultimately reduced to a mathematically simple model, whose two parameters can be determined by little more than visual inspection. The good fitting results obtained for all cases confirm the CLM as a good approximation to the generalized underlying principle governing amyloid fibrillization. A perspective is presented on possible applications of the CLM during the development of new targets for amyloid disease therapeutics. This model is hosted on BioModels Database and identified by: BIOMD0000000531. To cite BioModels Database, please use: BioModels Database: An enhanced, curated and annotated resource for published quantitative kinetic models. To the extent possible under law, all copyright and related or neighbouring rights to this encoded model have been dedicated to the public domain worldwide. Please refer to CC0 Public Domain Dedication for more information.

DISEASE(S): Alzheimer's Disease

SUBMITTER: Audald Lloret i Villas  

PROVIDER: BIOMD0000000531 | BioModels | 2014-07-17

REPOSITORIES: BioModels

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A generic crystallization-like model that describes the kinetics of amyloid fibril formation.

Crespo Rosa R   Rocha Fernando A FA   Damas Ana M AM   Martins Pedro M PM  

The Journal of biological chemistry 20120705 36


Associated with neurodegenerative disorders such as Alzheimer, Parkinson, or prion diseases, the conversion of soluble proteins into amyloid fibrils remains poorly understood. Extensive "in vitro" measurements of protein aggregation kinetics have been reported, but no consensus mechanism has emerged until now. This contribution aims at overcoming this gap by proposing a theoretically consistent crystallization-like model (CLM) that is able to describe the classic types of amyloid fibrillization  ...[more]

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