Spectroscopic analyses on interaction of bovine serum albumin with novel spiro[cyclopropane-pyrrolizin]

Yu, Xianyong; Liao, Zhixi; Jiang, Bingfei; Hu, Xiaolian; Li, Xiaofang

doi:10.1016/j.saa.2014.08.098

Cited by 11 publications

(6 citation statements)

References 36 publications

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“…Results of Table 2 indicate that the binding of BSA with PHs is remarkable and the effect of temperature, ranging from 293 K to 313 K, on the binding constant is also noticeable. Similar type of results considering novel spiro[cyclopropane-pyrrolizin]-BSA system was reported by Yu et al [10] . The binding constants of the interaction between PHs and BSA increase in the following order: PH-2< PH-1< PH-3, i.e., the compound PH-3 has the strongest ability to bind with BSA and compound PH-2 is the weakest.…”

Section: Resultssupporting

confidence: 87%

“…Earlier similar observations were also reported by other groups [7] , [40] , [41] . The forces between the novel spiro[cyclopropane-pyrrolizin]-BSA system were also found to be mainly H-bonds and van der Waals interactions according to Yu et al [10] .…”

Section: Resultsmentioning

confidence: 89%

“…Already in recent years few reports have been published regarding interaction between serum albumin and synthetic organic compounds [7] , [8] , [9] . Very recently, the interaction between novel spiro[cyclopropane-pyrrolizin] and BSA has been studied by Yu et al [10] . Wang et al [11] reported the interaction between clenbuterol hydrochloride and BSA.…”

Section: Introductionmentioning

confidence: 99%

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Binding interaction of phosphorus heterocycles with bovine serum albumin: A biochemical study

Roy

Nandi

Ganai

et al. 2017

Journal of Pharmaceutical Analysis

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Interaction between bovine serum albumin (BSA) and phosphorus heterocycles (PHs) was studied using multi-spectroscopic techniques. The results indicated the high binding affinity of PHs to BSA as it quenches the intrinsic fluorescence of BSA. The experimental data suggested the fluorescence quenching mechanism between PHs and BSA as a dynamic quenching. From the UV–vis studies, the apparent association constant (Kapp) was found to be 9.25×102, 1.27×104 and 9.01×102 L/mol for the interaction of BSA with PH-1, PH-2 and PH-3 respectively. According to the Förster's non-radiation energy transfer (FRET) theory, the binding distances between BSA and PHs were calculated. The binding distances (r) of PH-1, PH-2 and PH-3 were found to be 2.86, 3.03, and 5.12 nm, respectively, indicating energy transfer occurs between BSA and PHs. The binding constants of the PHs obtained from the fluorescence quenching data were found to be decreased with increase of temperature. The negative values of the thermodynamic parameters ΔH, ΔS and ΔG at different temperatures revealed that the binding process is spontaneous; hydrogen bonds and van der Waals interaction were the main force to stabilize the complex. The microenvironment of the protein-binding site was studied by synchronous fluorescence and circular dichroism (CD) techniques and data indicated that the conformation of BSA changed in the presence of PHs. Finally, we studied the BSA-PHs docking using Autodock and results suggest that PHs is located in the cleft between the domains of BSA.

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Section: Resultssupporting

confidence: 87%

Section: Resultsmentioning

confidence: 89%

Section: Introductionmentioning

confidence: 99%

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Binding interaction of phosphorus heterocycles with bovine serum albumin: A biochemical study

Roy

Nandi

Ganai

et al. 2017

Journal of Pharmaceutical Analysis

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“…K sv is quenching constant of Stern–Volmer. The temperature-dependent behavior of K sv can be used to judge quenching mechanisms . With increasing temperature, collisional quenching involved in the dynamic quenching mechanisms was increased because of the faster diffusion of molecules.…”

Section: Resultsmentioning

confidence: 99%

“…The temperature-dependent behavior of K sv can be used to judge quenching mechanisms. 43 With increasing temperature, collisional quenching involved in the dynamic quenching mechanisms was increased because of the faster diffusion of molecules. However, the decomposition of weakly bound complexes occurred with increasing temperature, which induced the decreasing of static quenching.…”

Section: Molecular Pharmaceuticsmentioning

confidence: 99%

Preparation of Curcumin–Piperazine Coamorphous Phase and Fluorescence Spectroscopic and Density Functional Theory Simulation Studies on the Interaction with Bovine Serum Albumin

Pang

et al. 2017

Mol. Pharmaceutics

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In the present study, a new coamorphous phase (CAP) of bioactive herbal ingredient curcumin (CUR) with high solubilitythe was screened with pharmaceutically acceptable coformers. Besides, to provide basic information for the best practice of physiological and pharmaceutical preparations of CUR-based CAP, the interaction between CUR-based CAP and bovine serum albumin (BSA) was studied at the molecular level in this paper. CAP of CUR and piperazine with molar ratio of 1:2 was prepared by EtOH-assisted grinding. The as-prepared CAP was characterized by powder X-ray diffraction, modulated temperature differential scanning calorimetry, thermogravimetric analysis, Fourier-transform infrared, and solid-state C nuclear magnetic resonance. The 1:2 CAP stoichioimetry was sustained by C═O···H hydrogen bonds between the N-H group of the piperazine and the C═O group of CUR; piperazine stabilized the diketo structure of CUR in CAP. The dissolution rate of CUR-piperazine CAP in 30% ethanol-water was faster than that of CUR; the t values were 243.1 min for CUR and 4.378 min for CAP. Furthermore, interactions of CUR and CUR-piperazine CAP with BSA were investigated by fluorescence spectroscopy and density functional theory (DFT) calculation. The binding constants (K) of CUR and CUR-piperazine CAP with BSA were 10.0 and 9.1 × 10 L mol at 298 K, respectively. Moreover, DFT simulation indicated that the interaction energy values of hydrogen-bonded interaction in the tryptophan-CUR and tryptophan-CUR-piperazine complex were -26.1 and -17.9 kJ mol, respectively. In a conclusion, after formation of CUR-piperazine CAP, the interaction forces between CUR and BSA became weaker.

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Aggregation‐induced emission enhancement of anthracene‐derived Schiff base compounds and their application as a sensor for bovine serum albumin and optical cell imaging

et al. 2018

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Three anthracene-based Schiff base complexes, R1-R3 (R1 = (E)-N´-((anthracen-10-yl)methylene)benzohydrazide; R2 = (E)-1-((anthracen-10-yl)methylene)-4-phenylsemicarbazide; and R3 = (E)-1-((anthracen-10-yl)methylene)-4-phenylthiosemicarbazide) were synthesized from 9-anthracenecarboxaldehyde, benzohydrazide, 4-phenylsemicarbazide and 4-phenylthiosemi-carbazide respectively, and characterized by various spectral techniques. The absorption spectral characteristics of R1-R3 were bathochromically tuned to the visible region by extending the π conjugation. These target compounds were weakly fluorescent in tetrahydrofuran (THF) solution because of rapid isomerization of the C=N double bond in the excited state. However, the aqueous dispersion of R1-R3 in the THF/water mixture by the gradual addition of water up to 90% resulted in an increase in the fluorescence intensity mainly due to aggregation-induced emission enhancement (AIEE) properties. The formation of nanoaggregates of R1-R3 were confirmed by scanning electron microscopy (SEM) and atomic force microscopy (AFM) techniques. The compounds R1-R3 are ideal probes for the fluorescence sensing of bovine serum albumin (BSA) and breast cancer cells by optical cell imaging.

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Spectroscopic analyses on interaction of bovine serum albumin with novel spiro[cyclopropane-pyrrolizin]

Cited by 11 publications

References 36 publications

Binding interaction of phosphorus heterocycles with bovine serum albumin: A biochemical study

Binding interaction of phosphorus heterocycles with bovine serum albumin: A biochemical study

Preparation of Curcumin–Piperazine Coamorphous Phase and Fluorescence Spectroscopic and Density Functional Theory Simulation Studies on the Interaction with Bovine Serum Albumin

Aggregation‐induced emission enhancement of anthracene‐derived Schiff base compounds and their application as a sensor for bovine serum albumin and optical cell imaging

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