Conserved water mediated H-bonding dynamics of Ser117 and Thr119 residues in human transthyretin-thyroxin complexation: Inhibitor modeling study through docking and molecular dynamics simulation

- One water molecule bridging Ser117 and Thr119 of transthyretin is conserved in X-ray and MD simulated structures.
- This conserved hydrophilic center plays a salient role in T4 (thyroxin)-TTR complexation.
- MD simulation and docking studies have been used for inhibitor design.
- Four thyroxin modified inhibitors have been designed using conserved water mimic inhibitor design protocol.
- Theoretical studies indicate the plausibility of Mod4 to act as better inhibitor.