Interaction of norfloxacin with bovine serum albumin studied by different spectrometric methods; displacement studies, molecular modeling and chemometrics approaches

Naseri, Abdolhossein; Hosseini, Soheila; Rasoulzadeh, Farzaneh; Rashidi, Mohammad-Reza; Zakery, Maryam; Khayamian, Taghi

doi:10.1016/j.jlumin.2014.08.031

Cited by 53 publications

(18 citation statements)

References 54 publications

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“…The fluorescence emission and UV–visible absorption spectra range was 250–350 nm at 298 K. It is a good detail that if the emission spectrum of the donor protein (BSA) expressively overlaps with the absorption spectrum of acceptor biomolecule (ETMTMHQC), the donor and acceptor are shows close and the high possibility of energy transfer between donors to accepter high degree. The energy transfer mostly depended on the overlapping area of spectra as well as the distance between the donor–acceptor molecules, whereas energy transfer efficiency ( E ) was calculated using the equation

E = 1 - \frac{F}{F_{0}} = \frac{R_{0}^{6}}{R_{0}^{6} + r^{6}}

where F 0 and F are the fluorescence intensities of BSA in the absence and presence of ETMTMHQC, respectively; r is the distance between the donor (BSA) and the acceptor (ETMTMHQC); and R 0 is 50% distance at which energy gets transferred and this R 0 value was calculated using the equation

R_{0}^{6} = 8.8 \times 10^{- 25} K^{2} n ϕ J (λ)

where K 2 is the space factor of orientation related to the geometry of the donor and acceptor dipoles, n is the average refractive index of the medium in the wavelength range where the n is significant spectral overlap between donor and acceptor spectra, ϕ is the fluorescence quantum yield of the donor in the absence of acceptor, and J expresses the degree of spectral overlap between the donor emission and the acceptor absorption which could be calculated by integrating the spectral overlap area in between 300 and 500 nm from the following equation

J = \frac{Σ F (λ) ε (λ) λ^{4} Δ λ}{Σ F (λ) Δ λ}

where F (λ) is the fluorescence intensity of the donor in the wavelength range λ and ε(λ) is the extinction coefficient of the acceptor at wavelength λ in M −1 cm −1 . For the present study, K 2 , φ, and n were taken as 2/3, 0.118, and 1.336, respectively.…”

Section: Methodsmentioning

confidence: 99%

In Vitro Study of Ethyl‐4‐(3,4.5‐trimethoxyphenyl)‐2,7,7‐trimethyl‐5‐oxo1,4,5,6,7,8‐hexahydroquinoline‐3‐carboxylate and Bovine Serum Albumin Using Multi‐Spectroscopic Techniques and Molecular Docking

Kumbhar¹,

Gore

Choudhari

et al. 2019

Macromolecular Symposia

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The binding of quinolone derivative ethyl‐4‐(3,4.5‐trimethoxyphenyl)‐2,7,7‐trimethyl‐5‐oxo1,4,5,6,7,8‐hexahydroquinoline‐3‐carboxylate (ETMTMHQC) to bovine serum albumin (BSA) is investigated by various spectroscopic methods and molecular docking analysis. The fluorescence quenching spectroscopic results show that ETMTMHQC bind to the protein BSA. The binding constant value is found to be 5.2 × 10−6 K (mol dm3). The thermodynamic parameter of the system shows increase in temperature with gradual decrease in Stern–Volmer quenching constant thereby indicating static quenching mode. Negative entropy and positive enthalpy indicate the hydrogen bonding interaction. The (r) distance between BSA and ETMTMHQC obtained from fluorescence resonance energy transfer is found to be 7.0 nm. The UV–visible spectra reveal the increase in absorbance on formation of BSA–ETMTMHQC complex. The CD spectral study indicates reduction of α‐helical structure in BSA and small changes in the tertiary structure of the protein. ETMTMHQC interacts strongly with BSA, and small changes in protein morphology are advised by molecular docking results. Moreover, docking results show that ETMTMHQC binds to BSA at ASN390 residue.

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E = 1 - \frac{F}{F_{0}} = \frac{R_{0}^{6}}{R_{0}^{6} + r^{6}}

R_{0}^{6} = 8.8 \times 10^{- 25} K^{2} n ϕ J (λ)

J = \frac{Σ F (λ) ε (λ) λ^{4} Δ λ}{Σ F (λ) Δ λ}

Section: Methodsmentioning

confidence: 99%

In Vitro Study of Ethyl‐4‐(3,4.5‐trimethoxyphenyl)‐2,7,7‐trimethyl‐5‐oxo1,4,5,6,7,8‐hexahydroquinoline‐3‐carboxylate and Bovine Serum Albumin Using Multi‐Spectroscopic Techniques and Molecular Docking

Kumbhar¹,

Gore

Choudhari

et al. 2019

Macromolecular Symposia

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“…Multivariate curve resolution–alternating least squares (MCR–ALS) is one of the current chemometrics approaches used for resolving the two‐way UV–vis data to improve the understanding of complex kinetic processes and extract equilibrium profiles of reacting species . The pure spectra and equilibrium concentrations of coexisting species can be directly processed by MCR–ALS, which is helpful to identify the reacting species involved .…”

Section: Introductionmentioning

confidence: 99%

“…The concentration changes of reaction components during the reaction process are unavailable by conventional spectroscopic methods. Hence, the MCR–ALS method was used to analyze the overlapped spectra of the reactive components and which has become more popular in recent years …”

Section: Introductionmentioning

confidence: 99%

Deciphering the intercalative binding modes of benzoyl peroxide with calf thymus DNA

2017

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The binding of benzoyl peroxide (BPO), a flour brightener, with calf thymus DNA (ctDNA) was predicted by molecular simulation, and this were confirmed using multi-spectroscopic techniques and a chemometrics algorithm. The molecular docking result showed that BPO could insert into the base pairs of ctDNA, and the adenine bases were the preferential binding sites which were validated by the analysis of Fourier transform infrared spectra. The mode of binding of BPO with ctDNA was an intercalation as supported by the results from ctDNA melting and viscosity measurements, iodide quenching effects and competitive binding investigations. The circular dichroism and DNA cleavage assays indicated that BPO induced a conformational change from B-like DNA structure towards to A-like form, but did not lead to significant damage in the DNA. The complexation was driven mainly by hydrogen bonds and hydrophobic interactions. Moreover, the ultraviolet-visible (UV-vis) spectroscopic data matrix was resolved by a multivariate curve resolution-alternating least-squares algorithm. The equilibrium concentration profiles for the components (BPO, ctDNA and BPO-ctDNA complex) were extracted from the highly overlapping composite response to quantitatively monitor the BPO-ctDNA interaction. This study has provided insights into the mechanism of the interaction of BPO with ctDNA and potential hazards of the food additive.

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“…Because of having multiple lipophilic binding sites located in subdomains IIA and IIIA, serum albumins are capable of transporting and distributing of endogenous and exogenous compounds like various ligands, vitamins, hormones, drugs, nutrients, food additives and other physiological substances [2][3][4][5][6][7]. With increasing the amount of binding affinity between these proteins and compounds, free concentration and the physiological activity of various materials such as drugs decreased in blood plasma.…”

Section: Introductionmentioning

confidence: 99%

Kinetic studies of bovine serum albumin interaction with PG and TBHQ using surface plasmon resonance

Fathi

Dolatanbadi

Rashidi

et al. 2016

International Journal of Biological Macromolecules

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Interaction of norfloxacin with bovine serum albumin studied by different spectrometric methods; displacement studies, molecular modeling and chemometrics approaches

Cited by 53 publications

References 54 publications

In Vitro Study of Ethyl‐4‐(3,4.5‐trimethoxyphenyl)‐2,7,7‐trimethyl‐5‐oxo1,4,5,6,7,8‐hexahydroquinoline‐3‐carboxylate and Bovine Serum Albumin Using Multi‐Spectroscopic Techniques and Molecular Docking

In Vitro Study of Ethyl‐4‐(3,4.5‐trimethoxyphenyl)‐2,7,7‐trimethyl‐5‐oxo1,4,5,6,7,8‐hexahydroquinoline‐3‐carboxylate and Bovine Serum Albumin Using Multi‐Spectroscopic Techniques and Molecular Docking

Deciphering the intercalative binding modes of benzoyl peroxide with calf thymus DNA

Kinetic studies of bovine serum albumin interaction with PG and TBHQ using surface plasmon resonance

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