Generic placeholder image

Current Medicinal Chemistry

Editor-in-Chief

ISSN (Print): 0929-8673
ISSN (Online): 1875-533X

Computational Studies on Transthyretin

Author(s): G. Ortore, A. Martinelli

Volume 19 , Issue 15 , 2012

Page: [2380 - 2387] Pages: 8

DOI: 10.2174/092986712800269344

Price: $65

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.

Keywords: Amyloid fibril, docking, SAR, computational chemistry, molecular dynamics, pharmacophoric model, transthyretin, virtual screening, screening, human amyloidosis


Rights & Permissions Print Export Cite as
© 2022 Bentham Science Publishers | Privacy Policy