Binding evaluation of human serum albumin and a Pd(II) bischelate complex bearing N,O-alanine and O,O-malonate ligands:
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ORIGINAL PAPER
Binding evaluation of human serum albumin and a Pd(II) bischelate complex bearing N,O‑alanine and O,O‑malonate ligands: synthesis, characterization, biological investigation and molecular docking Maryam Saeidifar1 · Reihaneh Sabbaghzadeh2 · Hassan Mansouri Torshizi3 · Ali Akbar Saboury4 Received: 2 March 2020 / Accepted: 13 July 2020 © Iranian Chemical Society 2020
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 Förster 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.
Electronic supplementary material The online version of this article (https://doi.org/10.1007/s13738-020-02005-x) contains supplementary material, which is available to authorized users. * Maryam Saeidifar [email protected] 1
Nanotechnology and Advanced Materials Department, Materials and Energy Research Center, Karaj, Iran
2
Department of Biology, Faculty of Sciences, Hakim Sabzevari University, Sabzevar, Iran
3
Department of Chemistry, University of Sistan and Baluchestan, Zahedan, Iran
4
Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
13
Vol.:(0123456789)
Journal of the Iranian Chemical Society
Graphic abstract
Keywords Pd(II) complex · Interaction · Human serum albumin · DAPI · Docking
Introduction The molecular design and synthesis of new transition metalbased complexes with improved anticancer therapeutics is one of the major goals in bioinorganic and biological chemistry. Palladium complexes (Pd(II) complexes) due to similarity of coordination chemistry with platinum compounds (Pt(II) complexes) might be utilized as an alternative to standard anticancer drugs such as cisplatin, carboplatin and other platinum complexes. However, ligand substitution reactions for palladium compounds are faster than platinum complexes. The
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