In vitro Interactions of Secnidazole and Its Iron (II), Copper (II) Complexes with Bovine Serum Albumin by Fluorescence Quenching Method

Hossain, Md. Jamal; Sultan, Zakir; Rashid, Mohammad A.; Kuddus, Ruhul

doi:10.3329/bpj.v23i1.45313

Cited by 5 publications

(7 citation statements)

References 16 publications

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“…The binding affinity and binding mode of the ligand are highly temperature dependent. The effect of nickel (II) and chromium (III) ions on binding constant was also observed from ▶table 3, where the binding parameters of the SD-BSA system were collected from the previous work, published by Hossain et al [35]. The binding affinity of SD-Ni (II) complex decreased 7.1 % at room temperature while increased 12.79 % and 50 % at 308 K and 318 K temperatures, respectively.…”

Section: Effect Of Metal Ions On Protein Bindingsmentioning

confidence: 92%

“…The computed distances of these both metal chelates from the Trp residue of the serum protein were obtained below 8 nm that indicated the energy transfer mode was from BSA to ligand (donor to acceptor) with high probability. As nonradioactive energy transfer is not strongly correlated with temperature variation [33], the research ▶table 3 Effects of metal ions upon drug-protein interaction by comparing of binding parameters at 298 K, 308 K and 318 K. The binding parameters of the SD-BSA system were acquired from the previous work, published by Hossain et al [35]. The binding constants (K b ) for the both metal complexes were found more than the parent compound secnidazole.…”

Section: Energy Transfer Profilementioning

confidence: 99%

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Transition Metal Chelation Augments the Half-life of Secnidazole: Molecular Docking and Fluorescence Spectroscopic Approaches

2020

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This current research aimed to establish the most required pharmacodynamics parameters of two transition metal complexes of an antimicrobial drug secnidazole. The spectroscopic fluorescence quenching strategy was outlined to evaluate the binding mechanism and binding affinity of nickel (II) and chromium (III) complexes of secnidazole with bovine serum albumin (BSA). The conformational modifications and the interacting patterns of the protein due to the interaction of the parent compound of the metal complexes have been investigated by molecular docking approach. The ligand-protein interactions were confirmed by the spectral quelling of the serum protein’s intensity in the presence of metal chelate of secnidazole. The quenching mechanism was an endothermic dynamic process. The calculated thermodynamic factors delineated van der Waals interactions mainly influenced the spontaneous process. The UV-fluorescence curves were studied to establish the energy transformation profile according to the Förster resonance energy transfer (FRET) theory. The double-logarithm plot exhibited the binding number that ensured the drug-protein interaction was at a 1:1 ratio. The compared binding constants dictated that both metal chelates gained higher binding affinity, longer half-life, and achieved the capacity to show the pharmacological effects by a lower dose than the parent molecule.

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Section: Effect Of Metal Ions On Protein Bindingsmentioning

confidence: 92%

Section: Energy Transfer Profilementioning

confidence: 99%

Transition Metal Chelation Augments the Half-life of Secnidazole: Molecular Docking and Fluorescence Spectroscopic Approaches

2020

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“…The aqueous drug concentrations ranged from 1 to 10 mM, while BSA concentration was fixed at 0.025% (w/v) BSA solution. Most of the 200–500 nm range of fluorescence emission spectra were reported at two distinct excitation wavelengths, 280 , and 293 nm 7 . In this current research, the prepared sample was scanned and repeated three times to record the emission fluorescence spectrum at around 340 nm.…”

Section: Methodsmentioning

confidence: 99%

“…Hence insight into these interactions of a new ligand with protein is a significant step for the drug development process 6 . As an in vitro model, bovine serum albumin (BSA) is widely used for studying drug–protein interaction since its molecular composition is almost 76% similar to that of human SA 7 . Besides, the drug–protein interaction causes the interference of the binding of other drugs due to conformational changes or overlap of the binding sites.…”

Section: Introductionmentioning

confidence: 99%

Interactions of linagliptin, rabeprazole sodium, and their formed complex with bovine serum albumin: Computational docking and fluorescence spectroscopic methods

Hossain

Sultan

Rashid

et al. 2021

Analytical Science Advances

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The foremost aim of this thermodynamic study was to evaluate the pharmacokinetics (PK) and pharmacodynamics (PD) profiles of linagliptin (LG), rabeprazole sodium (RS), and their 1:1 formed complex by interacting with bovine serum albumin (BSA) at physiological pH 7.4. The molecular interactions of these ligands with the desired biomolecule were substantiated by the spectral quelling of fluorescence intensity of BSA. The fluorescent test and molecular docking revealed that the quenching mechanism was a spontaneous and exothermic static process, and the protein gained its secondary structure due to the interactions. The spectroscopic method was exercised to determine the thermodynamic factors that supported the interactions mediated by van der Waals forces and hydrogen bonds. The activation energy of the formed complex was higher than its precursor drugs while interacting with BSA, and the energy transformation profiles were studied by UV-fluorescence overlaid curves according to Förster resonance energy transfer (FRET) theory. The double log plot verified that these ligands bound with protein at a 1:1 ratio, which was confirmed by the approximately estimated values of the binding parameters. The drastically lower value of the binding constant of the formed complex suggested the lower half-life as well as its triggered elimination rate from the cardiovascular system, which may be an initial indicator of the reduced hypoglycemic property of linagliptin. Moreover, the UV-vis and synchronous fluorescence spectroscopic methods affirmed the conformational changes of the BSA due to drug-protein complexation and polarity alterations in the microenvironment of disparate chromophores of the biomolecule.

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“…Most of the 295-400 nm range of fluorescence emission spectra were reported at 280 nm excitation wavelength. The test tubes containing the solution of BSA and the drug or its complexes were heated at least 10 min before the measurements (in fluorescence spectrophotometer F-7000) (Tanwir et al, 2012;Hossain et al, 2020b;Hossain et al, 2020c).…”

Section: Fluorescence Quenching For Profiling Ligandprotein Bindingmentioning

confidence: 99%

Iron (II) and Zinc (II) complexes of gemifloxacin mesylate: synthesis, characterization, serum binding profiling, and evaluation of antimicrobial activity

Aktar¹,

Hossain²,

Sultan³

et al. 2022

J Bangladesh Acad Sci

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Gemifloxacin mesylate is a synthetic fluoroquinolone derived antimicrobial agent. Two metal complexes of gemifloxacin mesylate were synthesized viz. gemifloxacin-Fe and gemifloxacin-Zn. The formed complexes were characterized by using TLC, TGA and FT-IR spectra analyses. The formed complexes were then evaluated for antimicrobial activity. The newly formed two complexes were assessed against nine bacterial and one fungal strain, where gemifloxacin (30 µg/disc) was used as a reference standard. The new complexes showed better activity than the standard reference drug against Klebsiella pneumoniae among nine bacterial strains. But two bacterial species, Acinetobacter lwoffii and Enterococcus faecium, and the fungal strain Candida albicans showed complete resistance to the newly synthesized complexes and the reference standard. The drug protein interaction with the Bovine Serum Albumin (BSA) was also studied. The interaction mechanism was explored, suggesting that gemifloxacin and its Zn (II) complex interact with BSA via a static process while the Fe (II) complex interacts via a dynamic process and the lower Ksv value also indicated that drug -BSA complexes were formed in ground-state. J. Bangladesh Acad. Sci. 46(2); 203-211: December 2022

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In vitro Interactions of Secnidazole and Its Iron (II), Copper (II) Complexes with Bovine Serum Albumin by Fluorescence Quenching Method

Cited by 5 publications

References 16 publications

Transition Metal Chelation Augments the Half-life of Secnidazole: Molecular Docking and Fluorescence Spectroscopic Approaches

Transition Metal Chelation Augments the Half-life of Secnidazole: Molecular Docking and Fluorescence Spectroscopic Approaches

Interactions of linagliptin, rabeprazole sodium, and their formed complex with bovine serum albumin: Computational docking and fluorescence spectroscopic methods

Iron (II) and Zinc (II) complexes of gemifloxacin mesylate: synthesis, characterization, serum binding profiling, and evaluation of antimicrobial activity

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