title: Computational studies on transthyretin.
abstract: Among the 23 different fibril proteins described in human amyloidosis, transthyretin is associated with the most common hereditary form of the disease and its knowledge is corroborated through about 150 crystal structures in addition to thousands of small ligands tested as fibril formation inhibitors. In spite of the large amount of available data, the mechanism of transthyretin aggregation and its inhibition through binding with small ligands is not clear. In the last decade, many groups of researchers have attempted to apply computational procedures to simulate these phenomena, with the aim of understanding them in depth and in order to rationalize the design of new promising inhibitors. A summary of the main molecular dynamics, docking, and structure-activity relationship studies carried out on transthyretin are reviewed here, and the most successful results and new trends are described in detail.
authors.affiliation: Dipartimento di Scienze Farmaceutiche, Università di Pisa, Italy. ortore@farm.unipi.it
authors.forename: G
authors.initials: G
authors.lastname: Ortore
authors.forename: A
authors.initials: A
authors.lastname: Martinelli
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D000686:Amyloidosis / Q000378:metabolism; D003198:Computer Simulation; D006801:Humans; D008958:Models, Molecular; D011228:Prealbumin / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D013329:Structure-Activity Relationship
chemical_list: D000682:Amyloid; D011228:Prealbumin