Molecular Dynamics Simulation Study of AG10 and Tafamidis Binding to the V122I Mutant of Transthyretin — Presentation Detail — Celebration of Scholars

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Jun Wang
Kim Instenes
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James Ripley

Molecular Dynamics Simulation Study of AG10 and Tafamidis Binding to the V122I Mutant of Transthyretin

Name: Riley Geoghegan
Major: Chemistry
Hometown: Crown Pont.
Faculty Sponsor: Kevin Morris
Other Sponsors: NIH grant #G12-MD007579, Howard University and NSF Grant #1709680
Type of research: SURE
Funding: SURE

Abstract

Familia Amyloidal Cardiomyopathy, FAC, is an amyloid disease in which amyloid fibrils aggregate into plaques and form in the heart, brain and lungs. It is caused by the mutation and subsequent misfolding of the protein Transthyretin (TTR). TTR is a free-moving transport protein produced in the liver and the choroid plexus. The mutation studied here was the Valine-122 to Isoleucine-122 (V122I) mutation. It is present 3% of the African American population. To study interactions between the ligand and the protein, molecular dynamics simulations were used to analyze the Ligand:Protein complex. The drug therapies studied were AG10 and DOAG10.

Poster file