Abstract
The water-soluble sodium alaninomalonatopalladate(II) complex (Na[Pd(Ala-Mal)]; PAM) was synthesized and characterized using elemental analysis, conductance, FTIR, 1H NMR, 13C NMR and UV–Vis spectroscopies. The HSA binding evaluation of PAM was carried out using fluorescence, absorption spectroscopic and molecular docking. Fluorescence studies revealed that PAM interacts with human serum albumin (HSA) through hydrogen binding and van der Waals interaction. Furthermore, the quenching mechanism followed by static and dynamic combination. However, absorption spectral study demonstrated that the dynamic quenching plays predominant role in binding process. 3D fluorescence studies confirmed alteration around tyrosine (Tyr) and tryptophan (Trp) residues, and the synchronous study indicated that Trp residues significantly contributed in interaction process. The distance between donor (HSA) and acceptor (PAM) was determined using Forster resonance energy transfer (FRET). Further, the potential antitumor activity of PAM against fibroblast normal cells, HFFF2, and breast cancer cells, MCF7, has proved the cytotoxic activity and apoptotic induction of PAM onto breast cancer cell lines with minimum effect on normal cells. Notably, in silico calculations confirmed the experimental results where hydrogen binding plays a major role in HSA and PAM interaction.
Published Version
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