Dataset Information

Masel2000 - Drugs to stop prion aggregates and other amyloids

ABSTRACT: Masel2000 - Drugs to stop prion aggregates and other amyloids Encoded non-curated model. Issues: - Missing initial concentration for species y, yb and z - Not reproducible figures This model is described in the article: Designing drugs to stop the formation of prion aggregates and other amyloids. Masel J, Jansen VA. Biophys. Chem. 2000 Dec; 88(1-3): 47-59 Abstract: Amyloid protein aggregates are implicated in many neurodegenerative diseases, including Alzheimer's disease and the prion diseases. Therapeutics to block amyloid formation are often tested in vitro, but it is not clear how to extrapolate from these experiments to a clinical setting, where the effective drug dose may be much lower. Here we address this question using a theoretical kinetic model to calculate the growth rate of protein aggregates as a function of the dose of each of three categories of drug. We find that therapeutics which block the growing ends of amyloids are the most promising, as alternative strategies may be ineffective or even accelerate amyloid formation at low drug concentrations. Our mathematical model can be used to identify and optimise an end-blocking drug in vitro. Our model also suggests an alternative explanation for data previously thought to prove the existence of an entity known as protein X. This model is hosted on BioModels Database and identified by: MODEL1410310000. 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): Huntington's Disease,Alzheimer's Disease,Parkinson's Disease

SUBMITTER: Audald Lloret i Villas

PROVIDER: MODEL1410310000 | BioModels | 2015-04-15

REPOSITORIES: BioModels

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			Action	DRS
	MODEL1410310000?filename=MODEL1410310000-biopax2.owl	Owl
	MODEL1410310000?filename=MODEL1410310000-biopax3.owl	Owl
	MODEL1410310000?filename=MODEL1410310000.m	Other
	MODEL1410310000?filename=MODEL1410310000.pdf	Pdf
	MODEL1410310000?filename=MODEL1410310000.png	Other

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Publications

Designing drugs to stop the formation of prion aggregates and other amyloids.

Masel J J Jansen V A VA

Biophysical chemistry 20001201 1-3

Amyloid protein aggregates are implicated in many neurodegenerative diseases, including Alzheimer's disease and the prion diseases. Therapeutics to block amyloid formation are often tested in vitro, but it is not clear how to extrapolate from these experiments to a clinical setting, where the effective drug dose may be much lower. Here we address this question using a theoretical kinetic model to calculate the growth rate of protein aggregates as a function of the dose of each of three categorie ...[more]

PMID: 11152275

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