Separate and simultaneous binding effects of aspirin and amlodipine to human serum albumin based on fluorescence spectroscopic and molecular modeling characterizations: A mechanistic insight for determining usage drugs doses

Abdollahpour, Nooshin; Asoodeh, Ahmad; Saberi, Mohammad Reza; Chamani, Jamshidkhan

doi:10.1016/j.jlumin.2011.04.043

Cited by 67 publications

(30 citation statements)

References 64 publications

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“…However, the undetectable fluorescence peaks of Tyr residues in the fluorescence spectrum of CML may indicate the energy transfer from Tyr to Trp in the emission [30]. The emission peaks showed a blue shift of 10 nm at 280 and 295 nm compared with the emission peak of free Trp (348 nm) [10], indicating the presence of Trp in a relatively hydrophobic region [31][32][33].…”

Section: Discussionmentioning

confidence: 98%

Conformational study reveals amino acid residues essential for hemagglutinating and anti-proliferative activities of <italic>Clematis montana</italic> lectin

Lu¹,

Zhang²,

Qi³

et al. 2014

ABBS

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Clematis montana lectin (CML), a novel mannose-binding lectin purified from C. montana Buch.-Ham stem (Ranunculaceae), has been proved to have hemagglutinating activity in rabbit erythrocytes and apoptosis-inducing activity in tumor cells. However, the biochemical properties of CML have not revealed and its structural information still needs to be elucidated. In this study, it was found that CML possessed quite good thermostability and alkaline resistance, and its hemagglutinating activity was bivalent metal cation dependent. In addition, hemagglutination test and fluorescence spectroscopy proved that GuHCl, urea, and sodium dodecyl sulfate could change the conformation of CML and further caused the loss of hemagglutination activity. Moreover, the changes of fluorescence spectrum indicated that the tryptophan (Trp) microenvironment conversion might be related to the conformation and bioactivities of CML. In addition, it was also found that Trp residues, arginine (Arg) residues, and sulfhydryl were important for the hemagglutinating activity of CML, but only Trp was proved to be crucial for the CML conformation. Furthermore, the Trp, Arg, and sulfhydrylmodified CML exhibited 97.17%, 76.99%, and 49.64% loss of its anti-proliferative activity, respectively, which was consistent with the alterations of its hemagglutinating activity. Given these findings, Trp residues on the surface of CML are essential for the active center to form substrate-accessible conformation and suitable environment for carbohydrate binding.

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Section: Discussionmentioning

confidence: 98%

Conformational study reveals amino acid residues essential for hemagglutinating and anti-proliferative activities of <italic>Clematis montana</italic> lectin

Lu¹,

Zhang²,

Qi³

et al. 2014

ABBS

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“…Values of the quenching constant (K sv ) as determined from the slope of the initial linear parts of the plots are given in Table 1 ) was obtained for warfarin-HSA interaction, which was similar to those reported earlier for other drugs, known to bind to site I of HSA. 28,29 Warfarin is known to bind to site I of HSA molecule. 8,9 There was a significant decrease in the K sv value with increasing urea concentrations (Table 1), which suggested the increase in the distance between excited fluorophore (Trp) and the ligand (warfarin), due to significant loss in the tertiary structure of the protein at higher urea concentrations.…”

Section: 27mentioning

confidence: 99%

Warfarin Binding to Native and Structurally-Altered Human Serum Albumins

Sakhaei¹,

Halim²,

Tayyab³

2015

IJPER

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Background and Purpose: Interaction of a drug with the carrier protein in the circulation determines its distribution, free or bound concentration and metabolism. Structural alteration in the major transport protein, human serum albumin (HSA) under several pathological conditions may affect its drug binding ability. The objective of the present investigation was to explore the binding of warfarin to structurally-altered HSA. Methods: Effect of urea, a denaturant on the interaction of warfarin with HSA was investigated using fluorescence spectroscopy. Results and Discussion: Fluorescence spectra of native HSA were characterized by the presence of an emission maximum around 339 and 343 nm, when excited at 280 and 295 nm, respectively. Warfarin binding to HSA was marked by a significant decrease in the fluorescence intensity and red shift in the emission maximum, being more pronounced at lower (1-5 µM) and smaller at higher (10-40 µM) drug concentrations. Presence of urea affected these signals to a significant extent even at lower concentrations. A significant decrease in both quenching and binding constants with increasing urea concentrations, suggested separation of excited fluorophore (Trp) of HSA and warfarin leading to the loss in its drug binding ability.

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“…For example, HSA can transport several endogenous and exogenous compounds, like fatty acids, nutrients, steroids, certain metal ions, hormones and drugs, and also significantly affect their biological activity in pharmacology through altering their pharmacokinetic properties [1][2][3][4][5][6][7]. Binding of drugs to plasma proteins may strongly influence their distribution and elimination [8], for instance, many drug candidates were rendered ineffective due to their unusually high binding affinity to HSA [9][10][11][12][13][14]. Therefore, investigation of the binding interaction between drugs and HSA is of importance in pharmacology and pharmacodynamics.…”

Section: Introductionmentioning

confidence: 99%

“…The results provide a quantitative understanding of fluorine substitution effects on FDQL-HSA interactions to some extent, which could be useful for further design of potential biologically active quinazolinone derivatives. elimination [8], for instance, many drug candidates were rendered ineffective due to their unusually high binding affinity to HSA [9][10][11][12][13][14]. Therefore, investigation of the binding interaction between drugs and HSA is of importance in pharmacology and pharmacodynamics.…”

Section: Introductionmentioning

confidence: 99%

Comparative Studies of Interactions between Fluorodihydroquinazolin Derivatives and Human Serum Albumin with Fluorescence Spectroscopy

Zhu

et al. 2016

Molecules

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Abstract:In the present study, 3-(fluorobenzylideneamino)-6-chloro-1-(3,3-dimethylbutanoyl)-phenyl-2,3-dihydroquinazolin-4(1H)-one (FDQL) derivatives have been designed and synthesized to study the interaction between fluorine substituted dihydroquinazoline derivatives with human serum albumin (HSA) using fluorescence, circular dichroism and Fourier transform infrared spectroscopy. The results indicated that the FDQL could bind to HSA, induce conformation and the secondary structure changes of HSA, and quench the intrinsic fluorescence of HSA through a static quenching mechanism. The thermodynamic parameters, ∆H, ∆S, and ∆G, calculated at different temperatures, revealed that the binding was through spontaneous and hydrophobic forces and thus played major roles in the association. Based on the number of binding sites, it was considered that one molecule of FDQL could bind to a single site of HSA. Site marker competition experiments indicated that the reactive site of HSA to FDQL mainly located in site II (subdomain IIIA). The substitution by fluorine in the benzene ring could increase the interactions between FDQL and HSA to some extent in the proper temperature range through hydrophobic effect, and the substitution at meta-position enhanced the affinity greater than that at para-and ortho-positions.

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Separate and simultaneous binding effects of aspirin and amlodipine to human serum albumin based on fluorescence spectroscopic and molecular modeling characterizations: A mechanistic insight for determining usage drugs doses

Cited by 67 publications

References 64 publications

Conformational study reveals amino acid residues essential for hemagglutinating and anti-proliferative activities of <italic>Clematis montana</italic> lectin

Conformational study reveals amino acid residues essential for hemagglutinating and anti-proliferative activities of <italic>Clematis montana</italic> lectin

Warfarin Binding to Native and Structurally-Altered Human Serum Albumins

Comparative Studies of Interactions between Fluorodihydroquinazolin Derivatives and Human Serum Albumin with Fluorescence Spectroscopy

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Separate and simultaneous binding effects of aspirin and amlodipine to human serum albumin based on fluorescence spectroscopic and molecular modeling characterizations: A mechanistic insight for determining usage drugs doses

Cited by 67 publications

References 64 publications

Conformational study reveals amino acid residues essential for hemagglutinating and anti-proliferative activities of &lt;italic&gt;Clematis montana&lt;/italic&gt; lectin

Conformational study reveals amino acid residues essential for hemagglutinating and anti-proliferative activities of &lt;italic&gt;Clematis montana&lt;/italic&gt; lectin

Warfarin Binding to Native and Structurally-Altered Human Serum Albumins

Comparative Studies of Interactions between Fluorodihydroquinazolin Derivatives and Human Serum Albumin with Fluorescence Spectroscopy

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Conformational study reveals amino acid residues essential for hemagglutinating and anti-proliferative activities of <italic>Clematis montana</italic> lectin

Conformational study reveals amino acid residues essential for hemagglutinating and anti-proliferative activities of <italic>Clematis montana</italic> lectin