Characterization of 6-mercaptopurine binding to bovine serum albumin and its displacement from the binding sites by quercetin and rutin

Ehteshami, M; Rasoulzadeh, Farzaneh; Mahboob, Soltanali; Rashidi, Mohammad-Reza

doi:10.1016/j.jlumin.2012.10.044

Cited by 52 publications

(22 citation statements)

References 32 publications

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“…As it has been mentioned previously, ALP possesses intrinsic fluorescence arising from Trp, Tyr and Phe residues. The particularities of Tyr and Trp residues in different environmental conditions can be investigated by setting the excitation and emission wavelength interval (Δλ) to 15 and 60 nm, respectively (Ehteshami et al 2013). The effects of heating on ALP synchronous fluorescence spectra are shown in Fig.…”

Section: Synchronous Spectrummentioning

confidence: 99%

Monitoring the heat-induced structural changes of alkaline phosphatase by molecular modeling, fluorescence spectroscopy and inactivation kinetics investigations

et al. 2015

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The heat induced conformational changes of calf alkaline phosphatase (ALP) were analyzed using different methods, based on fluorescence spectroscopy, m o l e c u l a r m o d e l i n g a n d i n a c t i v a ti o n s t u d i e s . Experimental studies were conducted in buffer solution in the temperature range between 25 and 70°C. Molecular dynamic (MD) simulation provided details on thermally induced changes in ALP structure, highlighting that heating favored the hydrophobic exposure and important alteration of the catalytic site above 60°C. Additional information to MD data were obtained by using different fluorescence spectroscopy methods, which revealed a complex mechanism of thermal denaturation. Therefore, the emissive properties indicated an unfolding of ALP at temperatures below 60°C, whereas at higher temperatures, the polypeptides chains fold leading to a higher exposure of Trp residues. In order to establish a structure-function relationship, the results were correlated with inactivation studies of ALP in buffer at pH 9.0. The inactivation data were fitted using a first-order kinetic model, resulting in an activation energy value of 207.26±21.68 kJ·mol −1 .

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Section: Synchronous Spectrummentioning

confidence: 99%

Monitoring the heat-induced structural changes of alkaline phosphatase by molecular modeling, fluorescence spectroscopy and inactivation kinetics investigations

et al. 2015

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“…Changes of polarity around the chromophore molecule can be explored by measurement of the possible shift in the maximum emission wavelength (Bi et al 2012). Therefore, the heat-induced changes in Trp and Tyr microenvironment were obtained by setting the excitation and emission wavelength interval (Δλ) to 60 and 15 nm, respectively (Ehteshami et al 2013). Synchronous fluorescence spectrum (SFS) at Δλ of 60 nm for β-Lg (a) and β-Lg-LA (b) are shown in Fig.…”

Section: Synchronous Fluorescence Spectroscopymentioning

confidence: 99%

Exploring the heat-induced structural changes of β-lactoglobulin -linoleic acid complex by fluorescence spectroscopy and molecular modeling techniques

et al. 2015

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Linoleic acid (LA) is the precursor of bioactive oxidized linoleic acid metabolites and arachidonic acid, therefore is essential for human growth and plays an important role in good health in general. Because of the low water solubility and sensitivity to oxidation, new ways of LA delivery without compromising the sensory attributes of the enriched products are to be identified. The major whey protein, β-lactoglobulin (β-Lg), is a natural carrier for hydrophobic molecules. The thermal induced changes of the β-Lg-LA complex were investigated in the temperature range from 25 to 85°C using fluorescence spectroscopy techniques in combination with molecular modeling study and the results were compared with those obtained for β-Lg. Experimental results indicated that, regardless of LA binding, the polypeptide chain rearrangements at temperatures higher than 75°C lead to higher exposure of hydrophobic residues causing the increase of fluorescence intensity. Phase diagram indicated an all or none transition between two conformations. The LA surface involved in the interaction with β-Lg was about 497 Ǻ 2 , indicating a good affinity between those two components even at high temperatures. Results obtained in this study provide important details about heat-induced changes in the conformation of β-Lg-LA complex. The thermal treatment at high temperature does not affect the LA binding and carrier functions of β-Lg.

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“…6-Mercaptopurine (6-MP), is derived from the prodrugazathiopurine that is non-enzymatically converted to 6-MP in tissues, is a purine analogue which has antineoplastic and immunosuppressant properties [1]. Since its approval as an antitumour drug from Food and Drug Administration (FDA) in 1953 [2], it has been widely used in the treatment of acute lymphoblastic leukemia (ALL), rheumatological disorders, prevention of rejection following organ transplantation and inflammatory diseases [3].…”

Section: Introductionmentioning

confidence: 99%

“…For instance, incorporation of 6-TG induces cytotoxicity mediated via G2/M and/or S phase arrest [7,8]. However, 6-MP undergoes a complex biotransformation by XO (Xanthine oxidase) and TPMT (thiopurine S methyl transferase) which limits its bioavailability and leads to incomplete and variable bioavailability (about 16-50%) [1,9], short plasma half-life (0.5-1.5 h) [10], moderate plasma protein binding (19-30%) [11] and narrows therapeutic index which in turn results in plummeting chemotherapeutic effect and life-threatening toxicity, mainly in the form of myelosuppression [12,3].…”

Section: Introductionmentioning

confidence: 99%

Anti-cancerous efficacy and pharmacokinetics of 6-mercaptopurine loaded chitosan nanoparticles

Kumar

Sanganal

Phani³

et al. 2015

Pharmacological Research

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Characterization of 6-mercaptopurine binding to bovine serum albumin and its displacement from the binding sites by quercetin and rutin

Cited by 52 publications

References 32 publications

Monitoring the heat-induced structural changes of alkaline phosphatase by molecular modeling, fluorescence spectroscopy and inactivation kinetics investigations

Monitoring the heat-induced structural changes of alkaline phosphatase by molecular modeling, fluorescence spectroscopy and inactivation kinetics investigations

Exploring the heat-induced structural changes of β-lactoglobulin -linoleic acid complex by fluorescence spectroscopy and molecular modeling techniques

Anti-cancerous efficacy and pharmacokinetics of 6-mercaptopurine loaded chitosan nanoparticles

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