Familial Amyloidal Cardiomyopathy (FAC) is a rare disorder caused by the deposition of amyloid plaques in the heart. FAC is caused by the dissociation, misfolding and aggregation of a mutated form the protein transthyretin.  The compounds tafamidis and AG10 have recently been shown to bind to TTR and inhibit its dissociation and aggregation into plaques.  This poster will present molecular dynamics simulation research aimed at characterizing how these ligands interact with the V122I transthyretin mutant.  The location and conformation of the ligands within the binding pocket and hydrogen bonding interactions between the ligands and the receptor will be presented.

Molecular dynamics simulation study of AG10 and tafamidis binding to the V122I mutant of transthyretin

2019 Spring National Meeting

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