IMR Press / FBL / Volume 13 / Issue 11 / DOI: 10.2741/2992

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on as a courtesy and upon agreement with Frontiers in Bioscience.

Open Access Article
Towards modeling of amyloid fibril structures
Show Less
1 Bioinformatics Research Center and Department of Computer Science, University of North Carolina at Charlotte, Charlotte, NC 28223, USA
2 Department of Biochemistry and Molecular Biology and Institute of Bioinformatics, University of Georgia, Athens, GA 30602, USA

*Author to whom correspondence should be addressed.

Academic Editor: Buyong Ma

Front. Biosci. (Landmark Ed) 2008, 13(11), 4039–4050;
Published: 1 May 2008
(This article belongs to the Special Issue Computaional studies of protein aggregation)

Amyloid fibrils are associated with a number of debilitating diseases, including Alzheimer's disease and variant Creutzfeldt-Jakob disease. The elucidation of the structure of amyloid fibrils is an important step toward understanding the mechanism of amyloid formation and developing therapeutic agents for amyloid diseases. Despite great interests and substantial efforts from various research communities, deriving high-resolution structures of amyloid fibrils remains a challenging problem, due to the insolubility and non-crystalline nature of the fibrils. An array of experimental methods, such as electron microscopy, fiber diffraction, hydrogen-deuterium exchange, solid-state NMR, electron paramagnetic resonance spectroscopy and biochemical approaches, have been explored to study the problem, having yielded considerable amount of, though still partial, information about the fibril conformation. Computational modeling techniques can be used to predict and build structural models of amyloid fibrils, utilizing the available experimental data. Here, we describe a few computational methods for modeling of aggregate and fibril structures with a focus on protein threading-based approaches and discuss the challenging issues ahead.

Back to top