Analysis of the interaction of a new series of rhodanine derivatives with bovine serum albumin by fluorescence quenching

Zhu, Yunfeng; Li, Bo; Yin, Henan; Ge, Shenguang; Yu, Jinghua

doi:10.1007/s00706-013-0991-x

Cited by 7 publications

(3 citation statements)

References 18 publications

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“…, the resonance light scattering intensities show a decreasing trend, indicating that an interaction between BSA and gliclazide occurred . The values of K q1 , K SV1 , n and K a1 can be obtained from equations and . The results are listed in Table , which shows that the values of K SV1 and K a1 decrease with increasing temperature, suggesting that the process is controlled mainly by a static quenching mechanism between BSA and gliclazide.…”

Section: Resultsmentioning

confidence: 98%

“…Serum albumin is the major protein in blood plasma and is well known for its ability to bind to and transport various ligands to specific sites, both exogenous and endogenous . It is very important to study the interaction between proteins and small molecules in order to understand the mechanism of interaction at the molecular level . Bovine serum albumin (BSA) is one of the most extensively studied proteins due to its high structural homology with human serum albumin.…”

Section: Introductionmentioning

confidence: 99%

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Using resonance light scattering and UV/vis absorption spectroscopy to study the interaction between gliclazide and bovine serum albumin

Zhang

Liu

et al. 2015

Luminescence

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At different temperatures (298, 310 and 318 K), the interaction between gliclazide and bovine serum albumin (BSA) was investigated using fluorescence quenching spectroscopy, resonance light scattering spectroscopy and UV/vis absorption spectroscopy. The first method studied changes in the fluorescence of BSA on addition of gliclazide, and the latter two methods studied the spectral change in gliclazide while BSA was being added. The results indicated that the quenching mechanism between BSA and gliclazide was static. The binding constant (Ka ), number of binding sites (n), thermodynamic parameters, binding forces and Hill's coefficient were calculated at three temperatures. Values for the binding constant obtained using resonance light scattering and UV/vis absorption spectroscopy were much greater than those obtained from fluorescence quenching spectroscopy, indicating that methods monitoring gliclazide were more accurate and reasonable. In addition, the results suggest that other residues are involved in the reaction and the mode 'point to surface' existed in the interaction between BSA and gliclazide. Copyright © 2015 John Wiley& Sons, Ltd.

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Section: Resultsmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

Using resonance light scattering and UV/vis absorption spectroscopy to study the interaction between gliclazide and bovine serum albumin

Zhang

Liu

et al. 2015

Luminescence

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“…As a major protein in blood plasma, serum albumin can transport various ligands to specific sites, both exogenous and endogenous (15). Understanding the interaction between proteins and small molecules would greatly promote deciphering the underlying mechanism (16). Bovine serum albumin, one of the serum albumin most diffusely researched, is highly structural homologous with human serum albumin (17,18), so it is continually adopted in biophysics and biochemical research, and BSA can bind to many small molecules from different categories, including dyes, drugs, and toxic chemicals (19)(20)(21).…”

Section: Discussionmentioning

confidence: 99%

Icariin Exerts Estrogen-Like Actions on Proliferation of Osteoblasts in Vitro via Membrane Estrogen Receptors-Mediated Non-nuclear Effects

Zhang

Yan

et al. 2022

Iran J Pharm Res

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Background: According to reports, icariin (ICA) is a bone anabolic agent able to prevent osteoporosis in both ovariectomized rats and postmenopausal women. However, its effect on osteoblast proliferation remains to be determined, and the underlying mechanism remains to be elucidated. Methods: Icariin-bovine serum albumin (BSA) conjugates were purified by Sephadex G-25 gel chromatography technology. Primary osteoblasts from neonatal rats were used to evaluate the effects of ICA, ICA-BSA, ICA-BSA + ICI182780, and ICA-BSA + PD98059. 3-(4,5-dimethyl-thiazol-2-yl)-2,5-diphenyl tetrazolium bromide (MTT) and propidium iodide (PI)-staining assays were used to detect the proliferation of osteoblasts after drug exposure. The intracellular calcium ions were detected using a confocal microscope with Fluo-3/AM as the fluorescent indicator. Western blot was capitalized on to measure the relative content of phospho-extracellular signal-regulated kinase (p-ERK). Results: Primary osteoblasts in culture were detected by histochemical staining of alkaline phosphatase, and calcified nodules were obtained by sequential digestion. Icariin and bovine serum albumin could form conjugate, which could be purified by Sephadex G-25 gel chromatography technology. MTT and flow cytometry results show that ICA-BSA conjugate significantly facilitated the proliferation of osteoblasts (P < 0.05). The intracellular calcium ions also ascended vastly in the cells treated with ICA-BSA conjugate (P < 0.01). Icariin-bovine serum albumin exposure rapidly activated the extracellular signal-regulated kinase (ERK) signaling. Furthermore, ICA- and ICA-BSA-mediated actions on osteoblasts were signally alleviated after dealing with ERK inhibitor PD98059 or estrogen receptor (ER) antagonist ICI182780, which might have a relation to the repression of ERK phosphorylation. Conclusions: Icariin could serve as estrogen in osteoblast cells by the rapid nongenomic ER signaling pathway independent of ligand and estrogen response element (ERE) and mediated by mitogen-activated protein kinase (MAPK).

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Spectral Characteristic and Preliminary Anticancer Activity in vitro of Selected Rhodanine‐3‐carboxylic Acids Derivatives

Stawoska

Tejchman

Mazuryk

et al. 2017

Journal of Heterocyclic Chem

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Selected rhodanine‐3‐carboxylic acids derivatives were synthesized to determine the influence of the structure and the length of the linker between the carboxyl group and the nitrogen atom (N‐3) in the 2‐thioxo‐4‐thiazolidinone ring on their activity, monitored via interactions with human serum albumin. Based on fluorescence studies, we concluded that the length of the linker has a limited impact on these interactions. Additionally, we proposed the static mechanism of quenching for all the tested compounds. These derivatives seem to possess an anticancer activity in the nanomolar range with 3 as the most potent compound in both A2780 and A2780cisR cell lines.

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Analysis of the interaction of a new series of rhodanine derivatives with bovine serum albumin by fluorescence quenching

Cited by 7 publications

References 18 publications

Using resonance light scattering and UV/vis absorption spectroscopy to study the interaction between gliclazide and bovine serum albumin

Using resonance light scattering and UV/vis absorption spectroscopy to study the interaction between gliclazide and bovine serum albumin

Icariin Exerts Estrogen-Like Actions on Proliferation of Osteoblasts in Vitro via Membrane Estrogen Receptors-Mediated Non-nuclear Effects

Spectral Characteristic and Preliminary Anticancer Activity in vitro of Selected Rhodanine‐3‐carboxylic Acids Derivatives

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