Study on the interaction between Besifloxacin and bovine serum albumin by spectroscopic techniques

Yu, Xianyong; Jiang, Bingfei; Liao, Zhixi; Jiao, Yue; Yi, Pinggui

doi:10.1016/j.saa.2015.04.023

Cited by 19 publications

(6 citation statements)

References 35 publications

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“…Plots of log(F 0 ÀF)/F against log(1/([Q]À[P] (F 0 ÀF)/F 0 )) are utilized to determine the values of K b and n from the intercept and the slope, respectively. As for the energy transfer, based on the Förster theory [31,34], the transfer efficiency is defined as follows:…”

Section: Analysis Of Fluorescence Quenching Between Ecg and Bsamentioning

confidence: 99%

“…1, the fluorescence intensity of BSA decreased with the increasing of ECG concentration in the model wine with or without ultrasonic irradiation. A characteristic fluorescence emission spectrum of BSA is displayed with a maximum value at the wavelength of 336 nm, which is mainly attributed to the tryptophan (Trp) residues [34]. By comparing the two top curves (fluorescence spectra) in Fig.…”

Section: Effect Of Ultrasound Frequency On the Fluorescence Quenching...mentioning

confidence: 99%

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Effect of ultrasound on the interaction between (−)-epicatechin gallate and bovine serum albumin in a model wine

Zhang

García‐Martín

2017

Ultrasonics Sonochemistry

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Ultrasound is considered as a potential novel technique for improving the quality of some wines. In this paper, a model wine firstly was constructed with the standards of (-)-epicatechin gallate (ECG) and bovine serum albumin (BSA) as target compounds. Then, the experiments were conducted to investigate the effect of ultrasonic irradiation on the binding properties between ECG and BSA including quenching mechanism, binding parameters, binding forces, energy transfer distance and conformational changes determined by spectral analysis. The results indicate that ultrasound definitely has some regular effects on the binding interaction of BSA and ECG, and can induced the conformation variation of BSA in the simulated wine, which may suggest that the ultrasound might be employed to modify the wine organoleptic property by regulating the interaction between phenolic compounds and proteins from the autolysis of yeasts, since they are similar to the standards of ECG and BSA, respectively.

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Section: Analysis Of Fluorescence Quenching Between Ecg and Bsamentioning

confidence: 99%

Section: Effect Of Ultrasound Frequency On the Fluorescence Quenching...mentioning

confidence: 99%

Effect of ultrasound on the interaction between (−)-epicatechin gallate and bovine serum albumin in a model wine

Zhang

García‐Martín

2017

Ultrasonics Sonochemistry

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“…Synchronous fluorescence spectroscopy is a common method to study protein conformation [ 47 ]. Synchronous fluorescence spectroscopy was obtained by simultaneous scanning at the excitation (λ ex ) and emission (λ em ) wavelengths with a constant wavelength interval (Δλ) between them [ 6 ].…”

Section: Resultsmentioning

confidence: 99%

Wheat Protein Hydrolysates Improving the Stability of Purple Sweet Potato Anthocyanins under Neutral pH after Commercial Sterilization at 121 °C

Feng,

Qiao,

et al. 2024

Foods

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Anthocyanins are prone to degradation and color fading after sterilization. This work examined the potential of wheat protein hydrolysates (WPHs, 40 g/L) in improving the stability of purple sweet potato anthocyanins (PSPAs) under a pH of 6.8 after sterilization at 121 °C followed by storage. Results showed that WPHs increased the thermal degradation half-life of PSPAs 1.65 times after sterilization. Compared to PSPAs alone, after being stored at 37 °C and 45 °C for 7 days, the retention concentration of PSPAs with WPHs was 5.4 and 32.2 times higher, and the color change of PSPAs with WPHs decreased from 6.19 and 10.46 to 0.29 and 0.77, respectively. AFM data, fluorescence and UV spectrograms indicated the formation of complexes between PSPAs and WPHs by hydrophobic attraction confirmed by zeta-potential data. PSPAs with WPHs had stable particle size and zeta potential, which may also significantly increase the concentrations after digestion and antioxidant power of PSPAs. This work indicated that the assembled PSPAs composite structure by WPHs significantly reduced the degradation of PSPAs at a pH of 6.8 after sterilization at 121 °C followed by long-term storage.

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“…Synchronous fluorescence spectra were employed to investigate the protein conformational changes. If the Δλ between the excitation wavelength and emission wavelength is set at 15 nm and 60 nm, the synchronous fluorescence spectra provide the characteristic information of tyrosine or tryptophan residues respectively [26,27]. Figure 4ab showed that their emission intensities decreased with increasing concentration of AR3, in addition, the fluorescence intensity of tryptophan is much stronger than that of tyrosine although the quenching by AR3 is to a similar degree.…”

Section: Fluorescence Quenching Studiesmentioning

confidence: 99%

“…k q can be calculated from K sv in biomolecule when τ 0 is known: k q =K sv /τ 0 . Since there is absorption at 280 nm by AR2 and AR3, the fluorescence was corrected [26,27,29] with the equation:…”

Section: Fluorescence Quenching Studiesmentioning

confidence: 99%

UV-Vis, Fluorescence and Molecular Docking Studies on the Binding of Bovine and Human Serum Albumins with Novel Anticancer Drug Candidates

Romu¹,

A²,

Chen³

et al. 2020

J Biochem Analyt Stud

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Volume 4 -Issue 1 SA is widely used as a model protein for the investigation of protein surface binding and drug binding mechanisms because of its unique microenvironment (~seven hydrophobic grooves on its surface), and because it acts as a universal receptor for many drug molecules [10,11]. Both BSA and HSA are studied extensively side by side for protein-protein or protein-drug interaction because of their 76% similar structural sequence homology (583 and 585 amino acid residues respectively) [12]. They both are a single chain globular protein containing three structurally homologues domains, I, II and III along with two sub-domains (A and B) within each. Two specific drug binding sites were identified in the hydrophobic cavities in the sub-domains, known as sites I (in subdomain IIA) and II (in subdomain IIIA) of albumin [13][14][15]. Protein fluorescence originates from amino acid residues such as tryptophan, tyrosine and phenylalanine present at these sites or from the fluorescence of the bound drug molecule itself. In BSA, the two dominant fluorescence sites are Trp 134 located on the surface of sub-domain IB, and Trp 212 located within the hydrophobic pocket of sub-domain IIA. The amino acids responsible for its intrinsic fluorescence in HSA are Trp 214 (most dominant) which resides in sub-domain IIA, and several tyrosine residues located in different sub-domains [14][15][16].Fluorescence spectroscopy is a commonly used analytical technique in the study of interactions between drugs and serum albumin because

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Study on the interaction between Besifloxacin and bovine serum albumin by spectroscopic techniques

Cited by 19 publications

References 35 publications

Effect of ultrasound on the interaction between (−)-epicatechin gallate and bovine serum albumin in a model wine

Effect of ultrasound on the interaction between (−)-epicatechin gallate and bovine serum albumin in a model wine

Wheat Protein Hydrolysates Improving the Stability of Purple Sweet Potato Anthocyanins under Neutral pH after Commercial Sterilization at 121 °C

UV-Vis, Fluorescence and Molecular Docking Studies on the Binding of Bovine and Human Serum Albumins with Novel Anticancer Drug Candidates

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