Research details on completed and undergoing projects are available here...

Amyloid fibril is the insoluble aggregate of usually solvable proteins or polypeptides. There are over 16 types of human diseases known to be associated with amyloidogenesis, such as Alzheimer, light-chain amyloidosis, spongiform encephalopathies, amyotropic lateral sclerosis. Although many advances have been made in structural characterization of amyloid fibrils and the mechanism of their formation, many aspects of this process remain unclear. Due to difficulties in crystallizing amyloid fibrils, the detailed intrinsic structure has yet to be determined from x-ray diffraction. Lack of knowledge of the detailed structure of amyloid fibril makes it difficult to understand aggregation mechanisms, and more importantly the origin of toxicity of many of such aggregates.

Due to limitations in computation power to study large protein systems in molecular dynamics simulations, We will employ the discrete molecular dynamics algorithm. We intend (i) to reconstruct macromolecular assemblies of two and more identical proteins in molecular dynamics simulations; (ii) to reconstruct the phase diagram of aggregation (the dependence of the speed of aggregation on the environment); (iii) to identify the mechanism of protein aggregation; (iv) to test the predicted from molecular dynamics simulations macromolecular assemblies via experimental collaborations; and (v) to study the toxicity of the predicted aggregates in vivo. All of these steps are vital for understanding the development of complex diseases, and specifically steps (i) and (ii) for identifying effective therapies.