Analysis of the spectroscopic characteristics on the binding interaction between tosufloxacin and bovine lactoferrin

Guo, Ming; Zhang, Luying; Lü, Wei-Jun; Cao, H.

doi:10.1016/j.jlumin.2010.11.036

Cited by 26 publications

(13 citation statements)

References 33 publications

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“…The Stern-Volmer relationship on a certain concentration condition suggested that a flexible fit effect may exist between FA and LF, as explained by Guo et al [26]. For a static quenching binding mechanism, the fluorescence data were analyzed based on Equation 2, and values for the binding The emission quenching data were collected for complexes involving the protein heat treated at different temperatures, followed by applying the Stern-Volmer model such as to confirm the quenching mechanism that occurs in the LF-FA systems (Table 1).…”

Section: Quenching Experimentsmentioning

confidence: 81%

“…The intrinsic fluorescence of LF excited at 295 nm is mainly due to the Trp residues, and ligands binding, such as FA, might interfere with fluorescence emission [26]. Several studies indicated that measuring the intrinsic fluorescence quenching of LF, allows collecting valuable data on the binding characteristics and the change in the microenvironment of the fluorophore within the macromolecule [27,28].…”

Section: Intrinsic Fluorescence Spectramentioning

confidence: 99%

See 1 more Smart Citation

Spectroscopic and Molecular Modeling Investigation on the Interaction between Folic Acid and Bovine Lactoferrin from Encapsulation Perspectives

Aprodu

Dumitraşcu

Râpeanu

et al. 2020

Foods

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The impact of thermal treatment on the ability of lactoferrin (FL) to bind folic acid (FA) was investigated by employing fluorescence spectroscopy, molecular dynamics and docking tests. The structural and conformational particularities of LF upon heating at 80 °C and 100 °C were first estimated based on the intrinsic fluorescence changes in respect to the native protein. The emission spectra indicated gradual unfolding events accompanied by Trp exposure with increasing temperature. In agreement with the experimental results, molecular modeling investigations showed that the secondary and tertiary structure of LF are slightly affected by the thermal treatment. Some minor unfolding events related particularly to the α-helical regions of LF were observed when the temperature increased to 100 °C. The LF fluorescence quenching upon FA addition indicated that a static mechanism stands behind LF-FA complex formation. Regardless of the simulated temperature, the hydrogen bonds played an important role in regulating the interaction between the protein and ligand. FA binding to LF equilibrated at different temperatures occurred spontaneously, and all complexes displayed good thermodynamic stability. The obtained results support the suitability of LF as biocompatible material, for obtaining micro- and nanoparticles for delivery of dietary supplements or for enhancing the functionality of target delivery systems.

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Section: Quenching Experimentsmentioning

confidence: 81%

Section: Intrinsic Fluorescence Spectramentioning

confidence: 99%

Spectroscopic and Molecular Modeling Investigation on the Interaction between Folic Acid and Bovine Lactoferrin from Encapsulation Perspectives

Aprodu

Dumitraşcu

Râpeanu

et al. 2020

Foods

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show abstract

“…LF is the main defense force to protect the eye from invasion which can cause various ocular surface diseases. In view of its important physiological functions, many drug molecules, such as lomefloxacin [ 5 ], tosufloxacin [ 6 ], oleic acid [ 7 ], and polyphenon [ 8 ], have been reported to interact with LF.…”

Section: Introductionmentioning

confidence: 99%

Studies on the Interaction between Three Small Flavonoid Molecules and Bovine Lactoferrin

Huang

Liu

et al. 2018

BioMed Research International

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The interaction between three flavonoids, i.e., Luteolin (LTL), Quercetin (QCT), and Naringenin (NGN) and bovine lactoferrin (BLF) at pH 7.4 was investigated by fluorescence quenching spectra, synchronous fluorescence spectra, and UV-visible absorption spectra. The results indicate the fluorescence of BLF quenched by Luteolin (LTL), Quercetin (QCT), and Naringenin (NGN) via static quenching. The main force between QCT and LTL with BLF was van der Waals interactions and hydrogen bonds. Electrostatic interactions played a major role in the binding process of interaction between NGN and BLF. Synchronous fluorescence was used to study the conformational changes of BLF. The values of binding constant (Ka) and number of binding sites (n) at different temperatures (300K, 305K, 310K) were also calculated, respectively. The results of corresponding thermodynamic parameters as well as binding distance between BLF and LTL, QCT, or GNG were obtained. These results implied that Luteolin (LTL), Quercetin (QCT), and Naringenin (NGN) could provide important guides for compound quantity (e.g., medicine dosage) and the design of new compounds (or drugs).

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“…These shifts revealed that the conformation of lactoferrin changed, the polarity around the tryptophan residues decreased, and the hydrophobicity increased with gallic acid, while the presence of chlorogenic acid or XOS modified the microenvironment from a nonpolar into a polar state; in other words, tryptophan residues were located in a less hydrophobic environment and were more exposed to the solution. 34 These shifts in the spectra expressed some changes in conformation of lactoferrin upon binding with gallic acid, chlorogenic acid, and XOS, respectively. The conformation of lactoferrin in lactoferrin−EGCG aggregate was not monitored when glucose, FOS, or collagen peptide was added, respectively, since no shifts in fluorescence quenching spectra and synchronous fluorescence spectra were found.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

Inhibition of the Aggregation of Lactoferrin and (−)-Epigallocatechin Gallate in the Presence of Polyphenols, Oligosaccharides, and Collagen Peptide

Yang

Liu

et al. 2015

J. Agric. Food Chem.

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The aggregation of lactoferrin and (-)-epigallocatechin gallate (EGCG) was inhibited by polyphenols, oligosaccharides, and collagen peptide in this study. Polyphenols, oligosaccharides, or collagen peptide can effectively prevent the formation of lactoferrin-EGCG aggregates, respectively. The addition sequence of lactoferrin, polyphenols (oligosaccharides or collagen peptide) and EGCG can affect the turbidity and particle size of the ternary complexes in the buffer solution; however, it hardly affected the ζ-potential and fluorescence characteristics. With either positive or negative charge, polyphenols and collagen peptide disrupted the formation of lactoferrin-EGCG aggregate mainly through the mechanism of its competition with EGCG molecules which surrounded the lactoferrin molecule surface with weaker binding affinities, forming polyphenols or a collagen peptide-lactoferrin-EGCG ternary complex; for neutral oligosaccharides, the ternary complex was generated mainly through steric effects, accompanied by a change in the lactoferrin secondary structure induced by gallic acid, chlorogenic acid, and xylo-oligosaccharide. Polyphenols, oligosaccharides, or collagen peptide restraining the formation of lactoferrin-EGCG aggregate could be applied in the design of clear products in the food, pharmaceutical, and cosmetic industries.

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Analysis of the spectroscopic characteristics on the binding interaction between tosufloxacin and bovine lactoferrin

Cited by 26 publications

References 33 publications

Spectroscopic and Molecular Modeling Investigation on the Interaction between Folic Acid and Bovine Lactoferrin from Encapsulation Perspectives

Spectroscopic and Molecular Modeling Investigation on the Interaction between Folic Acid and Bovine Lactoferrin from Encapsulation Perspectives

Studies on the Interaction between Three Small Flavonoid Molecules and Bovine Lactoferrin

Inhibition of the Aggregation of Lactoferrin and (−)-Epigallocatechin Gallate in the Presence of Polyphenols, Oligosaccharides, and Collagen Peptide

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