Investigation on the interaction of newly designed potential antibacterial Zn(II) complexes with CT-DNA and HSA

被引:14
|
作者
Mansouri-Torshizi, Hassan [1 ]
Khosravi, Fatemeh [1 ]
Ghahghaei, Arezou [2 ]
Shahraki, Somaye [3 ]
Zareian-Jahromi, Sareh [1 ]
机构
[1] Univ Sistan & Baluchestan, Dept Chem, Zahedan, Iran
[2] Univ Sistan & Baluchestan, Dept Biol, Zahedan, Iran
[3] Univ Zabol, Dept Chem, Zabol, Iran
来源
关键词
Zn(II) complexes; CT-DNA binding; HSA binding; fluorescence quenching; antibacterial activity; HUMAN SERUM-ALBUMIN; CALF THYMUS DNA; ANTIMICROBIAL ACTIVITY; PALLADIUM(II) COMPLEXES; BINDING PROPERTIES; METAL-COMPLEXES; ANTIOXIDANT ACTIVITY; GLYCINE DERIVATIVES; COPPER(II) COMPLEX; II COMPLEXES;
D O I
10.1080/07391102.2017.1363086
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Two Zn(II) complexes of formula [Zn(bpy)(Gly)]NO3 (I) and [Zn(phen)(Gly)]NO3 (II) (where bpy=2,2'-bipyridine, phen = 1,10-phenanthroline and Gly = glycine) were synthesized and characterized by elemental analysis, molar conductance measurements, UV-vis, FT-IR, and H-1 NMR spectra. The interaction ability of these complexes with calf thymus DNA was monitored using spectroscopic methods, including UV-vis absorption spectroscopy, ethidium bromide displacement, Fourier transform infrared, and electrophoretic mobility assay. Further, the human serum albumin interactions of complexes I and II were investigated using UV-vis absorption spectroscopy, fluorescence quenching, circular dichroism, and Fourier transform infrared. The results obtained from these analyses indicated that both complexes interact effectively with CT-DNA and HSA. The binding constant (K-b), the Stern-Volmer constant (K-sv), and the number of binding sites (n) at different temperatures were determined for CT-DNA and HSA. Also, the negative Delta H degrees and Delta S degrees values showed that both hydrogen bonds and van der Waals forces played major roles in the association of CT-DNA-Zn(II) and HSA-Zn(II) complex formation. The displacement experiments suggested that Zn(II)-complexes primarily bound to Sudlow's site II of HSA. The distance between the donor (HSA) and the acceptor (Zn(II) complexes) was estimated on the basis of the Forster resonance energy transfer (FRET) and the alteration of HSA secondary structure induced by the compounds were confirmed by FT-IR spectroscopy. The complexes follow the binding affinity order of I > II with DNA and II > I with HSA. Finally, Antibacterial activity of complexes I and II have been screened against gram positive and gram negative bacteria.
引用
收藏
页码:2713 / 2737
页数:25
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