A spectroscopic and molecular docking approach on the binding of tinzaparin sodium with human serum albumin

Yadav

J of Molecular Recognition

et al. 2020

The interaction of triazole substituted 4-methyl-7-hydroxycoumarin derivatives (CUM1-4) with serum albumin (bovine serum albumin [BSA] and human serum albumin[HSA]) have been studied employing ultraviolet-visible (UV-Vis), fluorescence, circular dichroism (CD) spectroscopy, and molecular docking methods at physiological pH 7.4.The fluorescence quenching occurred with increasing concentration of CUMs, and the binding constant of CUM derivatives with BSA and HSA obtained from fluorescence quenching experiment was found to be~10 4 L mol −1 . CD study showed conformational changes in the secondary structure of serum albumin upon titration of CUMs.The observed experimental results were further validated by theoretical studies involving density functional theory (DFT) and molecular docking. K E Y W O R D S circular dichroism, coumarin, fluorescence quenching, molecular docking, serum albumin

Section: Resultssupporting

confidence: 92%

Interaction of coumarin triazole analogs to serum albumins: Spectroscopic analysis and molecular docking studies

Yadav

J of Molecular Recognition

et al. 2020

“…One of the most routinely used equations is the Hill equation, since it can determine the correct stoichiometry for the binding sites of protein and ligands. 42 To determine the binding parameters between ZVFe NP and HSA, Equation 2 was used: 42 log…”

Section: Binding Parametersmentioning

confidence: 99%

Albumin binding, anticancer and antibacterial properties of synthesized zero valent iron nanoparticles

Anbouhi¹,

Esfidvajani²,

Nemati³

et al. 2018

IJN

BackgroundNanoparticles (NPs) have been emerging as potential players in modern medicine with clinical applications ranging from therapeutic purposes to antimicrobial agents. However, before applications in medical agents, some in vitro studies should be done to explore their biological responses.AimIn this study, protein binding, anticancer and antibacterial activates of zero valent iron (ZVFe) were explored.Materials and methodsZVFe nanoparticles were synthesized and fully characterized by X-ray diffraction, field-emission scanning electron microscope, and dynamic light scattering analyses. Afterward, the interaction of ZVFe NPs with human serum albumin (HSA) was examined using a range of techniques including intrinsic fluorescence, circular dichroism, and UV–visible spectroscopic methods. Molecular docking study was run to determine the kind of interaction between ZVFe NPs and HSA. The anticancer influence of ZVFe NPs on SH-SY5Y was examined by MTT and flow cytometry analysis, whereas human white blood cells were used as the control cell. Also, the antibacterial effect of ZVFe NPs was examined on Pseudomonas aeruginosa (ATCC 27853), Escherichia coli (ATCC 25922), and Staphylococcus aureus (ATCC 25923).ResultsX-ray diffraction, transmission electron microscope, and dynamic light scattering analyses verified the synthesis of ZVFe NPs in a nanosized diameter. Fluorescence spectroscopy analysis showed that ZVFe NPs spontaneously formed a complex with HSA through hydrogen bonds and van der Waals interactions. Also, circular dichroism spectroscopy study revealed that ZVFe NPs did not change the secondary structure of HSA. Moreover, UV–visible data presented that melting temperature (Tm) of HSA in the absence and presence of ZVFe NPs was almost identical. Molecular dynamic study also showed that ZVFe NP came into contact with polar residues on the surface of HSA molecule. Cellular assays showed that ZVFe NPs can induce cell mortality in a dose-dependent manner against SH-SY5Y cells, whereas these NPs did not trigger significant cell mortality against normal white bloods in the concentration range studied (1–100 µg/mL). Antibacterial assays showed a noteworthy inhibition on both bacterial strains.ConclusionIn conclusion, it was revealed that ZVFe NPs did not induce a substantial influence on the structure of protein and cytotoxicity against normal cell, whereas they derived significant anticancer and antibacterial effects.

“…ChemBio3D Ultra12.0 was used to construct the three dimensional structure of ligands. All bound water molecule and heteroatoms were removed, essential hydrogen atoms and Geisteger charges were added to the protein using AutoDock Tools . The implemented Lamarckian genetic algorithm (LGA) in AutoDock was used to find the possible conformation of the ligands upon binding with protein.…”

Section: Resultsmentioning

confidence: 99%

Insight into the interaction of benzothiazole tethered triazole analogues with human serum albumin: Spectroscopy and molecular docking approaches

Yadav

Dixit³

et al. 2019

Luminescence

The interaction of four benzothiazole tethered triazole analogues (MS43, MS70, MS71, and MS78) with human serum albumin (HSA) was investigated using various spectroscopic techniques (ultraviolet-visible (UV-vis) light absorption, fluorescence, circular dichroism (CD), molecular docking and density functional theory (DFT) studies). Fluorescence quenching constants (~10 12 ) revealed a static mode of quenching and binding constants (K b~1 0 4 ) indicating the strong affinity of these analogues for HSA. Further alteration in the secondary structure of HSA in the presence of these analogues was also confirmed by far UV-CD spectroscopy. The intensity loss in CD studied at 222 nm indicated an increase in random coil/β-sheet conformations in the protein. Binding energy values (MS71 (−9.3 kcal mol −1 ), MS78 (−8.02 kcal mol −1 ), MS70 (−7.16 kcal mol −1 ) and MS43 (−6.81 kcal mol −1 )) obtained from molecular docking revealed binding of these analogues with HSA. Molecular docking and DFT studies validated the experimental results, as these four analogues bind with HSA at site II through hydrogen bonding and hydrophobic interactions.