Interaction between ropinirole hydrochloride and aspirin with human serum albumin as binary and ternary systems by multi-spectroscopic, molecular modeling and zeta potential

Mahaki, Hanie; Memarpoor-Yazdi, Mina; Chamani, Jamshidkhan; Saberi, Mohammad Reza

doi:10.1016/j.jlumin.2012.06.051

Cited by 33 publications

(14 citation statements)

References 65 publications

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“…The fluorescence intensity of peak 2 was also reduced by 25.13%, 40.01%, 37.32% and 55.76%, respectively, indicating that peptide strand structures of BSA were changed as well. These results supported that the interaction between compounds 1 – 4 and BSA triggered slightly microenvironmental and conformational alterations in BSA [46,47]. Besides, the reduced fluorescence intensity of peak 1 with the order of 4 > 3 > 2 > MINS > 1 at room temperature provided further evidence of the effect of substituent groups.…”

Section: Resultssupporting

confidence: 68%

Spectroscopic Study on the Interaction between Naphthalimide-Polyamine Conjugates and Bovine Serum Albumin (BSA)

et al. 2015

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Abstract:The effect of a naphthalimide pharmacophore coupled with diverse substituents on the interaction between naphthalimide-polyamine conjugates 1-4 and bovine serum albumin (BSA) was studied by UV absorption, fluorescence and circular dichroism (CD) spectroscopy under physiological conditions (pH = 7.4). The observed spectral quenching of BSA by the compounds indicated that they could bind to BSA. Furthermore, caloric fluorescent tests revealed that the quenching mechanisms of compounds 1-3 were basically static type, but that of compound 4 was closer to a classical type. The Ksv values at room temperature for compound-BSA complexes-1-BSA, 2-BSA, 3-BSA and 4-BSA were 1.438 × 10 and thermodynamic parameter suggested that the binding between compounds 1-4 with BSA protein, significantly affected by the substituted groups on the naphthalene backbone, was formed by hydrogen bonds, and other principle forces mainly consisting of charged and hydrophobic interactions. Based on results from the analysis of synchronous three-dimensional fluorescence and CD spectra, we can conclude that the interaction between compounds 1-4 and BSA protein has little impact on the BSA conformation. Calculated results obtained from in silico molecular simulation showed that compound 1 did not prefer either enzymatic drug sites I or II over the other. However, DSII in BSA was more beneficial than DSI for the binding between compounds 2-4 and BSA protein. The binding between compounds 1-3 and BSA was hydrophobic in nature, compared with the electrostatic interaction between compound 4 and BSA.

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Section: Resultssupporting

confidence: 68%

Spectroscopic Study on the Interaction between Naphthalimide-Polyamine Conjugates and Bovine Serum Albumin (BSA)

et al. 2015

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“…From different degrees of intensity changes of peak 1 and peak 2, the decrease of fluorescence intensity of the two peaks was consistent with the result of synchronous fluorescence spectra. These results showed that the interaction between MINS and BSA induced some microenviron and conformational alterations in BSA [48,49].…”

Section: (5) Three-dimensional Fluorescence Spectroscopy Analysismentioning

confidence: 82%

Spectroscopic study on the interaction between mononaphthalimide spermidine (MINS) and bovine serum albumin (BSA)

Tian

Zang

Luo

et al. 2015

Journal of Photochemistry and Photobiology B: Biology

102

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“…Synchronous fluorescence spectroscopy gives information about the molecular environment in the vicinity of the chromophore molecules. Its advantages are sensitivity, spectral simplification, spectral bandwidth reduction and the possibility of avoiding various perturbing effects . By investigating the synchronous fluorescence spectra of tyrosine and tryptophan residues, conformational changes in HSA structure can be explored.…”

Section: Resultsmentioning

confidence: 99%

Influence of quercetin on the interaction of gliclazide with human serum albumin – spectroscopic and docking approaches

et al. 2017

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Protein-binding interactions are displacement reactions which have been implicated as the causative mechanisms in many drug-drug interactions. Thus, the aim of presented study was to analyse human serum albumin-binding displacement interaction between two ligands, hypoglycaemic drug gliclazide and widely distributed plant flavonoid quercetin. Fluorescence analysis was used in order to investigate the effect of substances on intrinsic fluorescence of human serum albumin (HSA) and to define binding and quenching properties of ligand-albumin complexes in binary and ternary systems, respectively. Both ligands showed the ability to bind to HSA, although to a different extent. The displacement effect of one ligand from HSA by the other one has been described on the basis of the quenching curves and binding constants comparison for the binary and ternary systems. According to the fluorescence data analysis, gliclazide presents a substance with a lower binding capacity towards HSA compared with quercetin. Results also showed that the presence of quercetin hindered the interaction between HSA and gliclazide, as the binding constant for gliclazide in the ternary system was remarkably lower compared with the binary system. This finding indicates a possibility for an increase in the non-bound fraction of gliclazide which can lead to its more significant hypoglycaemic effect. Additionally, secondary and tertiary structure conformational alterations of HSA upon binding of both ligands were investigated using synchronous fluorescence, circular dichroism and FT-IR. Experimental data were complemented with molecular docking studies. Obtained results provide beneficial information about possible interference upon simultaneous co-administration of the food/dietary supplement and drug.

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Interaction between ropinirole hydrochloride and aspirin with human serum albumin as binary and ternary systems by multi-spectroscopic, molecular modeling and zeta potential

Cited by 33 publications

References 65 publications

Spectroscopic Study on the Interaction between Naphthalimide-Polyamine Conjugates and Bovine Serum Albumin (BSA)

Spectroscopic Study on the Interaction between Naphthalimide-Polyamine Conjugates and Bovine Serum Albumin (BSA)

Spectroscopic study on the interaction between mononaphthalimide spermidine (MINS) and bovine serum albumin (BSA)

Influence of quercetin on the interaction of gliclazide with human serum albumin – spectroscopic and docking approaches

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