Title:Molecular Dynamic Simulation and Spectroscopic Investigation of Some Cytotoxic Palladium(II) Complexes Interaction with Human Serum Albumin
VOLUME: 17 ISSUE: 9
Author(s):Mahboube Eslami Moghadam, Maryam Saidifar, Faramarz Rostami-Charati, Davoud Ajloo and Maryam Ghadamgahi
Affiliation:Chemistry & Chemical Engineering Research Center of Iran, Tehran, Iran.
Keywords:Glycine derivatives, HSA denaturation, molecular dynamics simulation, Pd(II) complex.
Abstract:Studies on the interactions between metallodrugs and human serum albumin (HSA), as carrier for drugs and
biological molecules, are extremely important to design and discover new drugs. The interaction of three novel
synthesized complexes of [Pd(phen)(R-gly)]NO3, where R-gly is methyl-, propyl-, and amyl-glycine and phen is 1,10-
phenanthroline, with HSA were investigated using spectroscopic studies in combination with a molecular dynamic
simulation. These water soluble complexes can denature HSA at ~50 µM. According to the results obtained for the
isothermal titration at 27 and 37°C, it was found that there are 10, 8, and 6 binding sites (g) for methyl-, propyl-, and
amyl-glycine complexes on the HSA with positive cooperativity in binding, respectively. Also, the binding and
thermodynamic parameters were analyzed. We found a good consistency between secondary structure and simulation data
with spectroscopic studies, and the experimental data are confirmed by molecular simulation results. In addition, the
results related to helix, beta sheets, and coil percentages revealed that all complexes decrease the helix structure and
increase the beta structure; and that the amyl derivative is more effective in denaturing the HSA structure.
