Protein-flavonol interaction: Fluorescence spectroscopic study

Guharay, Jayanti; Sengupta, Bidisa; Sengupta, Pradeep K.

doi:10.1002/1097-0134(20010501)43:2<75::aid-prot1019>3.0.co;2-7

Cited by 173 publications

(96 citation statements)

References 23 publications

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“…BSA has been best studied due to its structural homology with HSA [14,15]. The BSA molecule consists of three homologous domains (I, II, III), which are separated into nine loops (L1-L9) by disulfide bonds.…”

Section: Results and Discussion Fluorescent Analysis Of Interaction mentioning

confidence: 99%

“…According to crystallography data [15], 67% of the structure is represented by an ( helix with flexible sections between domains without β structure. BSA has two tryptophan residues with intrinsic fluorescence: Trp-134 (on the surface) in domain I, and Trp-212 (in a hydrophobic pocket) in domain II [14]. In contrast to BSA, in the structure of HSA there is only one tryptophan residue at the 214 position, which is located in a hydrophobic pocket [14].…”

Section: Results and Discussion Fluorescent Analysis Of Interaction mentioning

confidence: 99%

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Fluorescent analysis of interaction of flavonols with hemoglobin and bovine serum albumin

Sentchouk

Bondaryuk

2007

J Appl Spectrosc

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We have studied the fluorescent properties of flavonols (quercetin, fisetin, morin, rutin) with the aim of studying possible interaction with hemoglobin and bovine serum albumin (BSA). We observed an increase in the intensity of intrinsic fluorescence for all the flavonols except rutin in the presence of BSA. From the changes in the fluorescence spectra, we concluded that tautomeric forms are formed on interaction with hemoglobin. We determined the interconnection between the structure of related flavonols and their fluorescent properties on interaction with proteins, and we determined the binding constants for binding with BSA and hemoglobin.Introduction. Flavonols (quercetin, rutin, etc.) are among a number of biologically active natural compounds which display antioxidant, antiradical, angioprotective, and other types of activity [1]. These data are the basis for effective application of flavonols as the basis for a wide variety of drugs and biologically active food additives [1,2]. Results of pharmacokinetic studies show that flavonols are efficiently absorbed in the digestive tract and enter the systemic blood flow, and then are distributed to the organs and tissues [1,3]. Accordingly, there is interest in studying the interaction of flavonols with hemoglobin and serum albumin, which as we know transport many natural and synthetic biologically active compounds through the circulatory system [4]. Relatively recently, information has been published on participation of erythrocytes in transport of natural flavonoids [5]. In that paper, accumulation of quercetin was observed in erythrocytes by means of simple diffusion. In this case, inhibition of quercetin transport into cells in the presence of serum albumin was observed. As a result, the authors suggested the possibility that hemoglobin and albumin bind quercetin. But in many aspects, this protein-ligand interaction remains poorly studied to date. In the literature, there is information about the change in fluorescence for only quercetin when interacting with serum albumin [6][7][8][9]. Scattered and often fragmentary information has been published with regard to other flavonols [6,9].In this work, our task has been to study the fluorescent properties of a number of structurally related flavonols both in the free state and in the presence of the most important blood proteins (hemoglobin and bovine serum albumin (BSA)), with the aim of identifying possible interaction between them. Earlier [10] we carried out preliminary studies of the dependence of intrinsic fluorescence of flavonols on the conditions in the medium.We used the most widely distributed natural flavonols with well known biological activity: quercetin (3,5,7,3′,4′-pentaoxyflavone), rutin (3-rutinoside of quercetin), fisetin (5-deoxyquercetin), and morin (structural isomer of quercetin). We proposed to establish interactions between the structure of related flavonols and their fluorescent properties on interaction with hemoglobin and BSA.The Experiment. For the study, we used reagents from Sigma ...

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Section: Results and Discussion Fluorescent Analysis Of Interaction mentioning

confidence: 99%

Section: Results and Discussion Fluorescent Analysis Of Interaction mentioning

confidence: 99%

Fluorescent analysis of interaction of flavonols with hemoglobin and bovine serum albumin

Sentchouk

Bondaryuk

2007

J Appl Spectrosc

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“…20 Figure 5a reveals that fluorescence of HSA at 348 nm decreases with an increasing of FCLA concentration. The energy from excited-state HSA is likely transferred to FCLA or is lost by non-irradiation.…”

Section: Intermolecular Energy Transfer In Chemiluminescence Systemmentioning

confidence: 99%

A Novel Chemiluminescence Technique for Quantitative Measurement of Low Concentration Human Serum Albumin

Wei

Xing

et al. 2008

ANAL. SCI.

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An efficient and highly sensitive chemiluminescence (CL) technique is proposed in the current study for detection of low levels of human serum albumin (HSA). Chemiluminescence (CL) produced during interaction between fluoresceinyl cypridina luciferin analog (FCLA)-1 O2 can be modified with the presence of HSA. The conventional CL technique uses a quenching effect of HSA for its quantitative measurement. We are reporting here that the CL intensity can be enhanced, rather than quenched, by the addition of HSA. The CL signal can be linearly correlated with the HSA concentration over a clinically interesting range of 5 × 10 -9 -8 × 10 -8 mol L -1 , with a detection limit of 2.5 × 10 -9 mol L -1 . The determination result was consistent with that obtained from conventional methods. One possible mechanism of HSA detection technique using CL enhancement approach is discussed. Intermolecular energy transfer in chemiluminescence systems and changes of microenvironment are likely to be contributors of the CL enhancement with HSA.

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“…The spectroscopic properties of these fluorescence bands and the interplay of their intensities are strongly governed by the structure of the 3-hydroxychromone chromophore, which assign these a wide variety of high technological utility. Many 3-HCs have been synthesized and analysed for the development of new fluorescent probes for solvent polarity [2][3][4], ionic binding [5] and electric fields [6,7] with applications in the field of polymers [8], reverse micelles [9,10], host-guest complexes [11], lipid vesicles [7,[12][13][14][15], cellular membranes [16] and proteins [17][18][19][20][21]. These molecules have also been found to show fascinating photochemistry furnishing the oxirane scaffold [22].…”

Section: Introductionmentioning

confidence: 99%

Absorption and Fluorescent Studies of 3-Hydroxychromones

et al. 2015

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The synthesis and spectral studies of variously substituted 3-hydroxychromones have been carried out. A key relationship between the structural motif of synthesized 3-hydroxychromones (3-HCs) and their fluorescent properties was found. The chromones substituted with electron-donating group at 4'-position expressed the red shift of the N(*) and T(*) band and also exhibited the increased fluorescent intensity ratio while the chromones with electron-withdrawing group showed the blue shift of the N(*) and T(*) band. Therefore, these 3-HCs may behave as the possible fluorescent probes.

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Protein-flavonol interaction: Fluorescence spectroscopic study

Cited by 173 publications

References 23 publications

Fluorescent analysis of interaction of flavonols with hemoglobin and bovine serum albumin

Fluorescent analysis of interaction of flavonols with hemoglobin and bovine serum albumin

A Novel Chemiluminescence Technique for Quantitative Measurement of Low Concentration Human Serum Albumin

Absorption and Fluorescent Studies of 3-Hydroxychromones

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