This project investigated the binding of small molecules to the protein transthyretin (TTR). TTR transports thyroid hormones in the bloodstream. The protein is a tetramer consisting of four monomers, all of which contain 127 amino acids. Mutated forms of the tetramer can dissociate into monomers that are then susceptible to aggregating into amyloid fibrils that deposit around the heart. These fibrils build up in the cardiac muscle and can cause diastolic dysfunction and lead to heart failure. The destabilizing Valine-122 to Isoleucine-122 mutation was studied here. This point mutation is common amongst older adults and about 3% of African Americans. In this study, Molecular Dynamics (MD) simulations were used to investigate the binding of the compound piceatannol (PIC) to TTR. PIC is derived from resveratrol-a natural product found in grapes and other plants. Our hypothesis was that when PIC binds to TTR it stabilizes the TTR tetramer and thus could potentially prevent its dissociation and aggregation into amyloid fibrils. The MD simulations demonstrated that piceatannol interacted with both TTR Serine-117 and Leucine-110 residues. Importantly, these interactions occurred with different TTR monomers. Therefore, the MD simulations suggest that as hypothesized the PIC ligand holds the tetramer together, by interacting with residues on different monomers. Structures of PIC bound to TTR will be presented along with studies to identify the mechanism of TTR stabilization by piceatannol.