Investigation of the association behaviors between biliverdin and bovine serum albumin by fluorescence spectroscopy

Wei, Yan li; Li, Jian qing; Dong, Chuan; Shuang, Shao Min; Liu, Dian sheng; Huie, Carmen W.

doi:10.1016/j.talanta.2006.02.052

Cited by 126 publications

(56 citation statements)

References 26 publications

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“…Furthermore, it can be inferred from the values of n that there is an independent class of binding sites on HSA for captopril. Otherwise, it appears that the binding constants and the number of binding sites increased with increase in temperature [29,30]. This may be attributed to that the capacity of captopril binding to the fact that HSA is increased with increase in temperature.…”

Section: Fluorescence Quenching Spectra and Quenching Mechanism Of Hsmentioning

confidence: 99%

Analysis of Binding Interaction between Captopril and Human Serum Albumin

Gao¹,

Tang²,

Rong³

et al. 2011

AJAC

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The interaction between captopril, an inhibitor of angiotensin converting enzyme and human serum albumin, a principal plasma protein in the liver has been investigated in vitro under a simulated physiological condition by UV-vis spectrophotometry and fluorescence spectrometry. The intrinsic fluorescence intensity of human serum albumin was strongly quenched by captopril. The binding constants and the number of binding sites can be calculated from the data obtained from fluorescence quenching experiments. The negative value of G 0 reveals that the binding process is a spontaneous process. According to the van't Hoff equation, the standard enthalpy change (H 0 ) and standard entropy change (S 0 ) for the reaction were calculated to be 35.98 KJmol -1 and 221.25 Jmol -1 K. It indicated that the hydrophobic interactions play a main role in the binding of captopril to human serum albumin. In addition, the distance between captopril (acceptor) and tryptophan residues of human serum albumin (donor) was estimated to be 1.05 nm according to the Förster's resonance energy transfer theory. The results obtained herein will be of biological significance in pharmacology and clinical medicine.

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Section: Fluorescence Quenching Spectra and Quenching Mechanism Of Hsmentioning

confidence: 99%

Analysis of Binding Interaction between Captopril and Human Serum Albumin

Gao¹,

Tang²,

Rong³

et al. 2011

AJAC

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“…Otherwise, it appears that the binding constants and the number of binding sites increase with higher temperature. 20,21) This may be because the capacity of PUFX binding to HSA is enhanced with increasing temperature.…”

Section: )mentioning

confidence: 99%

Investigation on the Interaction of Prulifloxacin with Human Serum Albumin: A Spectroscopic Analysis

Huang

Wang

et al. 2010

CHEMICAL & PHARMACEUTICAL BULLETIN

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Proteins are important in living beings and take part in almost all life processes. They are not only involved in metabolism, immunity, and life evolution but also offer much information about ourselves. Human serum albumin (HSA), the most abundant protein in plasma, acts as a transporter and disposer of many endogenous and exogenous compounds.1-3) HSA consists of a single polypeptide chain of 585 amino acid residues and comprises three structurally homologous domains: I (residues 1-195); . It comprises three contiguous domains, each containing two subdomains (A and B) that possess common structural motifs conferred by various intra-and interdomain forces such as salt bridges and hydrophobic interactions. 4,5) The primary function of HSA lies in the maintenance of colloid osmotic pressure within blood vessels. HSA also acts as a carrier for transporting numerous hydrophobic molecules, e.g., steroid hormones, bilirubin, and fatty acids. Due to these properties, HSA is used clinically to treat severe hypoalbuminemia or traumatic shock. 6) Prulifloxacin (PUFX), 1,6-fluoro-1-methyl-7-[4-(5-methyl-2-oxo-1,3-dioxolen-4-yl)methy-1-piperazinyl]-4-oxo-4H- [1,3]thiaceto[3,2-a]quinoline-3-carboxylic acid, is a new type of oral antibiotic. It is a new thiazeto-quinolone antibacterial agent prodrug of the quinolone carboxylic acid ulifloxacin, characterized by potent, and broad-spectrum antibacterial activity. It is active against both gram-positive and gram-negative bacteria and several anaerobic and atypical bacteria associated with chronic bronchitis and urinary tract infections. 7,8) PUFX contains a quinolone skeleton with a fourmember ring in the 1, 2 position including a sulfur atom to increase antibacterial activity and an anoxodioxolenylmethyl group in the 7-piperazine ring to improve oral absorption. Determination of the active metabolite of prulifloxacin in human plasma using HPLC was reported. 9)In this paper, we report our studies on the interaction of PUFX with HSA using fluorescence spectrometry. Synchronous fluorescence measurement was employed to probe conformational changes induced by PUFX. Binding parameters were calculated according to fluorescence data, and the binding mode is discussed based on thermodynamic analysis. The precise location of PUFX on HSA was identified in competitive binding experiments and further calculated based on fluorescence resonance energy transfer (FRET). ExperimentalApparatus and Reagents An FP-6500 fluorescence spectrometer (Jasco, Japan) was used to record the fluorescence spectra. Absorption spectra were recorded on a TU1901 UV/Vis Spectrophotometer (PGeneral, Beijing, China). The pH values of Britton-Robinson (B-R) buffer solutions were measured with a PHS-23 meter (Shanghai Secondly Analytical Instruments, P. R. China).PUFX solution (1.0ϫ10 Ϫ4 mol/l) (99.0% purity) was prepared by dissolving PUFX 0.0461 g (461.46 Da, Shanghai Modern Pharmaceutical, Shanghai, P. R. China) in 1000 ml of deionized water. HSA (1.0ϫ10 Ϫ4 mol/l) was prepared by dissolving 3.3250 g of HSA (66500 D...

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“…The synchronous fluorescence spectra provide information about the molecular environment in the vicinity of the chromosphere molecules and the changes of maximum emission wavelength reflect the conformational changes of BSA (22). When the ∆λ between excitation wavelength and emission wavelength was fixed at 15 and 60 nm, the synchronous fluorescence spectra gave the characteristic information of tyrosine and tryptophan residues, respectively (23).…”

Section: Conformational Investigationsmentioning

confidence: 99%

Spectroscopic studies on the interaction of efonidipine with bovine serum albumin

Wang

Zhao

et al. 2008

Braz J Med Biol Res

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Efonidipine hydrochloride is an antihypertensive and antianginal agent with fewer side effects and is better tolerated in the treatment of hypertension with renal impairment. Its interaction with bovine serum albumin (BSA) is of great use for the understanding of the pharmacokinetic and pharmacodynamic mechanisms of the drug. The binding of efonidipine to BSA was investigated by fluorescence spectroscopy and circular dichroism. BSA fluorescence was quenched by efonidipine, due to the fact that efonidipine quenched the fluorescence of tryptophan residues mainly by the collision mode. The thermodynamic parameters ∆H 0 and ∆S 0 were 68.04 kJ/mol and 319.42 J·mol -1 ·K -1 , respectively, indicating that the hydrophobic interactions played a major role. The results of circular dichroism and synchronous fluorescence measurements showed that the binding of efonidipine to BSA led to a conformational change of BSA. The fraction of occupied sites (θ) for the 8-anilino-1-naphthaleinsulfonic acid (ANS)-BSA system is 85%, whereas for the NZ-105-BSA system, it is 53%, which suggests that the interaction of ANS with BSA is stronger than that of NZ-105 with BSA. Binding studies in the presence of ANS indicated that efonidipine competed with ANS for hydrophobic sites of BSA. The effects of metal ions on the binding constant of the efonidipine-BSA complex were also investigated. The presence of metal ions Zn 2+ , Mg 2+ , Al 3+ , K + , and Ca 2+ increased the binding constant of efonidipine-BSA complex, which may prolong the storage period of NZ-105 in blood plasma and enhance its maximum effects.

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Investigation of the association behaviors between biliverdin and bovine serum albumin by fluorescence spectroscopy

Cited by 126 publications

References 26 publications

Analysis of Binding Interaction between Captopril and Human Serum Albumin

Analysis of Binding Interaction between Captopril and Human Serum Albumin

Investigation on the Interaction of Prulifloxacin with Human Serum Albumin: A Spectroscopic Analysis

Spectroscopic studies on the interaction of efonidipine with bovine serum albumin

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