Transthyretin (TTR) is a tetramer protein, and it is one of around 30 non-homologic amyloidogenic human proteins related to amyloid diseases. The diseases related to TTR amyloid include familial amyloid cardiomyopathy (FAC), familial amyloid polyneuropathy (FAP), senile systemic amyloidosis (SSA), and central nervous system-selective amyloidosis (CNSA). These diseases are proposed to be due to the formation of TTR amyloid and the construction of cross-β -sheet subunit via TTR misfolding. In this review, we describe the physiological characteristics and structural features of TTR, and summarize computational studies on TTR using molecular dynamics simulation, molecular docking and quantitative structure-activity relationships. These computational chemical studies demonstrate possible mechanisms of TTR amyloid formation and the binding abilities of small molecules and TTR, which may provide insights to discover and screen new inhibitors preventing TTR from misfolding.

Contents
1 Introduction
1.1 Physiological function and structural charac-teristics of TTR
1.2 Diseases caused by misfolding of TTR
1.3 Mechanisms of amyloid formation
1.4 Treatment of amyloid diseases
2 Molecular dynamic simulation on TTR
2.1 The mechanisms of TTR amyloid formation
2.2 The binding modes of small molecules with TTR
3 Molecular docking studies on TTR
4 Quantitative structure-activity relationship studies on TTR
5 Outlook