Probing the interaction of fisetin with human serum transferrin via spectroscopic and molecular docking approaches

Sandu, Nicoleta; Popescu, A.; Chilom, Claudia G.

doi:10.1080/07391102.2021.1934545

Cited by 7 publications

(3 citation statements)

References 22 publications

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“…From the Equation (1), the efficiency of energy transfer, E, was determined, E = 0.12, and also, the distance between HST and Fh-NPs was found to be 3.18 nm. This value, in agreement with the rule 0.5R0 < r < 1.5R0, confirms that simple Fh-NPs quenched the HST fluorescence via a static process [7]. The parameters were listed in Table 3, together with the parameters determined for Cu-Fh-NPs-HST and Co-Fh-NPs-HST.…”

Section: Fluorescence Resonance Energy Transfer From Hst To the Ferri...supporting

confidence: 85%

“…𝛥𝐺 = −𝑅𝑇 𝑙𝑛 𝐾 = 𝛥𝐻 − 𝑇𝛥𝑆 (7) where Kb is the association constant; T is the absolute temperature; R is the gas constant (8.314 J K −1 mol −1 ).…”

Section: 𝑙𝑛mentioning

confidence: 99%

“…The reference value for an adult is in the range 250-400 µg/dL and 30% is saturated with iron [4,5]. In addition to transporting iron, HST binds and transports a wide variety of molecules such as flavonoids [6,7] and vitamins [8]. HST may be a candidate for functionalized NPs to target cancer cells as they have an increased demand for iron and stimulate TFRC expression [9].…”

Section: Introductionmentioning

confidence: 99%

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Interactions of Chemically Synthesized Ferrihydrite Nanoparticles with Human Serum Transferrin: Insights from Fluorescence Spectroscopic Studies

Chilom

Sandu

Iftimie

et al. 2021

IJMS

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Human serum transferrin (HST) is a glycoprotein involved in iron transport that may be a candidate for functionalized nanoparticles to bind and target cancer cells. In this study, the effects of the simple and doped with cobalt (Co) and copper (Cu) ferrihydrite nanoparticles (Fh-NPs, Cu-Fh-NPs, and Co-Fh-NPs) were studied by spectroscopic and molecular approaches. Fluorescence spectroscopy revealed a static quenching mechanism for all three types of Fh-NPs. All Fh-NPs interacted with HST with low affinity, and the binding was driven by hydrogen bonding and van der Waals forces for simple Fh-NPs and by hydrophobic interactions for Cu-Fh-NPs and Co-Fh-NPs binding, respectively. Of all samples, simple Fh-NPs bound the most to the HST binding site. Fluorescence resonance energy transfer (FRET) allowed the efficient determination of the energy transfer between HST and NPs and the distance at which the transfer takes place and confirmed the mechanism of quenching. The denaturation of the HST is an endothermic process, both in the case of apo HST and HST in the presence of the three types of Fh-NPs. Molecular docking studies revealed that Fh binds with a low affinity to HST (Ka = 9.17 × 103 M−1) in accord with the fluorescence results, where the interaction between simple Fh-NPs and HST was described by a binding constant of 9.54 × 103 M−1.

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Section: Fluorescence Resonance Energy Transfer From Hst To the Ferri...supporting

confidence: 85%

“…𝛥𝐺 = −𝑅𝑇 𝑙𝑛 𝐾 = 𝛥𝐻 − 𝑇𝛥𝑆 (7) where Kb is the association constant; T is the absolute temperature; R is the gas constant (8.314 J K −1 mol −1 ).…”

Section: 𝑙𝑛mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Interactions of Chemically Synthesized Ferrihydrite Nanoparticles with Human Serum Transferrin: Insights from Fluorescence Spectroscopic Studies

Chilom

Sandu

Iftimie

et al. 2021

IJMS

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Investigation on the Interaction of Dy(Ш)/Rutin Complexes with Bovine Serum Albumin by Spectroscopic Methods

Liu

et al. 2021

J Solution Chem

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Spectroscopic and molecular docking approach of the interaction of vitamins with human serum transferrin

2022

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Probing the interaction of fisetin with human serum transferrin via spectroscopic and molecular docking approaches

Cited by 7 publications

References 22 publications

Interactions of Chemically Synthesized Ferrihydrite Nanoparticles with Human Serum Transferrin: Insights from Fluorescence Spectroscopic Studies

Interactions of Chemically Synthesized Ferrihydrite Nanoparticles with Human Serum Transferrin: Insights from Fluorescence Spectroscopic Studies

Investigation on the Interaction of Dy(Ш)/Rutin Complexes with Bovine Serum Albumin by Spectroscopic Methods

Spectroscopic and molecular docking approach of the interaction of vitamins with human serum transferrin

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