Analysis of dynamic characteristics of human serum albumin binding site
residues and its effect on azapropazone binding to HSA
Abstract
Background: Human serum albumin (HSA) is the most abundant protein in
the circulatory system compared to other proteins and has been analyzed
in a wide range of studies. In this research, molecular dynamics and
docking of HSA with azapropazone have been simulated. Methods: The
three-dimensional structure of human serum albumin was obtained to
simulate molecular dynamics from RCSB. GROMACS was used for molecular
dynamic simulations and received 30 frames. Autodock vina was used for
docking between HSA and Azapropazone. Results: Based on the obtained
results, the residues of Sudlow I junction have structural changes
according to their chemical properties. Conclusion: In this study, a new
method has been used on HSA compared to previous studies that can be
used in drug design research. Understanding the structural and
behavioral characteristics of HSA binding site can be a great help in
drug design because structural changes in binding amino acids affect
drug binding