Interactions of different polyphenols with bovine serum albumin using fluorescence quenching and molecular docking

Skrt, Mihaela; Benedik, Evgen; Podlipnik, Črtomir; Ulrih, Nataša Poklar

doi:10.1016/j.foodchem.2012.06.114

Cited by 227 publications

(121 citation statements)

References 32 publications

Supporting

Mentioning

103

Contrasting

Order By: Relevance

“…5 Hill's coefficient is a vital tool in analyzing the cooperativity (positive, negative and non-cooperative) of the binding of luteolin and quercetin respectively to BSA. 10 The data below indicated a mostly non-cooperative nature of binding (under our defined experimental conditions) ( Table 4 , 5b and 6a and 6b) was performed to determine the alterations in the secondary structure of BSA following a separate binding experiment with Luteolin and Quercetin respectively. There were IR peaks observed in the pure BSA sample at around 3300/cm which suggests medium intensity Alkene/Aromatic C-H stretching.…”

Section: Resultsmentioning

confidence: 99%

“…16 Fluorescence spectroscopy results seem to point towards a static quenching mechanism under our defined experimental conditions (Table 1a and 1b). 5,7,8,10,13,14,17 There have been very few reports wherein a comparison has been made between luteolin and quercetin with respect to fluorescence spectroscopy data. 13,17 Unlike the experimental flow in these reports, we have adopted an experimental design wherein thermodynamic and docking data have also been incorporated (please see below).…”

mentioning

confidence: 99%

See 1 more Smart Citation

A Correlative Multi-Spectroscopy and Docking Study for the Modeling of Drug (Luteolin and Quercetin) Binding to Bovine Serum Albumin– A Tool for the Determination of Binding Characteristics to Receptor Proteins

Krishnan¹,

Hiray²,

Vyas³

2018

IJPER

View full text Add to dashboard Cite

The in vitro in silico experimental flow (multi-spectroscopy and docking) demonstrated the binding of Luteolin and Quercetin separately with Bovine Serum Albumin. For the first time, we are reporting the relative UV-visible spectroscopy-based hypsochromic shifts for both luteolin (3nm) and quercetin (4.1 nm) respectively. The drug-induced conformational change may lead to the possible shift in the tryptophan residue to a more hydrophobic environment. Our demonstration of an increased static quenching of the endogenous fluorophore in BSA validated the UV-visible spectroscopy data. However, detailed experiments will further delineate the possible relative contribution of dynamic quenching processes. The strong binding (binding constant values -10 5 L/mol) and the number of binding sites (1 for luteolin and quercetin) is consistent with published findings. Under our defined conditions, the hitherto unreported non-cooperative binding was demonstrated, based on the Hill's coefficient. Thermodynamic data qualitatively validated hydrophobicity (a positive entropy change ΔS 0 ); hydrogen bonding (a negative ΔH 0 ) and electrostatic interactions (a negative ΔH 0 and a positive ΔS 0 ). For the first time, the Infra-Red Spectroscopy (FT-IR) data showed ground state complex formation of the molecules with the model protein and may serve to corroborate our fluorescence (static quenching) data. Hydrogen bonds and hydrophobic interactions for both molecules (Ligplot Analysis) provide corroborative evidence for the molecular spectroscopy and thermodynamic data. This hitherto unreported, unique, combinatorial in vitro (multispectroscopy and thermodynamic measurements) in silico (docking and Ligplot-based analysis) experimental flow (specifically for luteolin and quercetin) provides a basis for extending such binding studies for novel receptors and/or ligands.

show abstract

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

A Correlative Multi-Spectroscopy and Docking Study for the Modeling of Drug (Luteolin and Quercetin) Binding to Bovine Serum Albumin– A Tool for the Determination of Binding Characteristics to Receptor Proteins

Krishnan¹,

Hiray²,

Vyas³

2018

IJPER

View full text Add to dashboard Cite

show abstract

“…The method reported by Skrt et al (2011) was followed with slight modifications. The glycated samples were diluted 200 times with PBS to measure the amount of fluorescent AGEs (AGE-fl) by using a Hitachi FL-4600 fluorometer at excitation and emission wavelengths of 370 and 440 nm, respectively.…”

Section: Methodsmentioning

confidence: 99%

Contribution of linoleic acid to the formation of advanced glycation end products in model systems during heat treatment

Zhao¹,

Lu²,

Liu³

et al. 2017

Czech J. Food Sci.

View full text Add to dashboard Cite

Zhao X., Yue L., Liu X., Liu L. (2017): Contribution of linoleic acid to the formation of advanced glycation end products in model systems during heat treatment. Czech J. Food Sci., 35: 367-375.Advanced glycation end products (AGEs) are glycosylated metabolic products generated in vivo and are associated with aging-related diseases. They are also formed during heat treatment in food processing. In this work, we investigated the contribution of linoleic acid (LA) to AGE formation using a protein/glucose model. An electronic tongue, denaturing polyacrylamide gel electrophoresis, electron spin resonance spectroscopy, circular dichroism, and ultraperformance liquid chromatography-tandem mass spectrometry were used to analyse reaction intermediates and reactive radical formation. The results show that LA is the key factor responsible for the change in flavour including the rapid triggering of glycation reactions. The amount of lipid-induced reactive radicals was significantly higher than in the non-fat system, radical generation in the non-fat system was gradually quenched after a robust radical-yielding reaction in the first 25 minutes. Subsequent unsaturated lipid oxidation, and AGE accumulation surpass Maillard reaction-only outcomes. Initial LA-induced changes in protein structure are followed by glycation and are enhanced by hydrophobic interactions and increased carbonyl levels resulting from lipid oxidation. These findings implicate lipids and lipid oxidation as the main factors responsible for AGE formation during the processing of fat-rich unsaturated fatty acid-containing foods.

show abstract

“…Each galloyl group provides three hydroxyl groups which can potentially interact with the catalytic site amino acid side-chains of amylase (Asp 197 , Glu 233 and Asp 300 ) (Fei et al, 2014) upon the formation of hydrogen bonds, while the benzene ring may develop hydrophobic π-π (aromatic-aromatic) interactions in the active site of amylase (Miao, Jiang, Jiang, Li, Cui, & Jin, 2013;Skrt, Benedik, Podlipnik, & Ulrih, 2012). In addition, in the galloyl group the C=O double bond is conjugated to the benzene ring and is responsible for electron delocalization, which has been proposed to lead to enhanced π-π interactions with the indole ring of Trp 59 (Lo Piparo, Scheib, Frei, Williamson, Grigorov, & Chou, 2008).…”

Section: Discussionmentioning

confidence: 99%

“…Therefore, the relieving effect of the polysaccharides on PPA inhibition was mainly attributed to the interactions between polysaccharides and polyphenols, rather than that between polysaccharides and PPA. (Cai, Yu, Xu, Liu, & Yang, 2015;Skrt, Benedik, Podlipnik, & Ulrih, 2012), and a higher value of K FQ also suggests greater binding interactions between them. Therefore, the fluorescence quenching results provide further evidence that the three polysaccharides weaken the binding of tea polyphenols with PPA, as the values of K FQ ' (in the presence of polysaccharides) were lower than that of K FQ (in the absence of polysaccharides) (Table 5.2).…”

Section: Discussionmentioning

confidence: 99%

Studying the interactions between tea polyphenols and α-amylase

Sun¹

View full text Add to dashboard Cite

Dixon, Cornish-Bowden and Lineweaver-Burk plot analyses were applied to study the detailed kinetics of inhibition of porcine pancreatic α-amylase (PPA) by tea polyphenols.Fluorescence quenching (FQ), differential scanning calorimetry (DSC) and isothermal titration calorimetry (ITC) were combined with the kinetics of inhibition to elucidate the mechanism of binding interactions of tea polyphenols and PPA. Then, the reciprocal of competitive inhibition constant (1/K ic ), fluorescence quenching constant (K FQ ) and binding constant (K itc ) obtained from these measurements were compared and correlated to analyse the relations between PPA inhibition and binding behaviour. The role of the galloyl moiety in binding of catechins and theaflavins with PPA was highlighted as well. In addition, the effects of three soluble polysaccharides (citrus pectin (CP), wheat arabinoxylan (WAX) and oat β-glucan (OBG)) on the inhibition of PPA by tea polyphenols were studied through PPA inhibition, IC 50 value, inhibition kinetics and fluorescence quenching methods. Furthermore, the effects of tea polyphenols on binding of PPA with normal maize starch granules were studied in terms of binding ratio, dissociation constant (K d ) and binding rate. Then, the association constant (1/K d ), 1/K ic and K FQ of tea polyphenols were correlated to analyse the effects of PPA inhibition on the binding of the enzyme with starch.The results show that green, oolong and black tea extracts, epigallocatechin gallate, theaflavin-3, 3'-digallate and tannic acid were competitive inhibitors of PPA, whereas epicatechin gallate, theaflavin-3'-gallate and theaflavin were mixed-type inhibitors with both competitive and uncompetitive inhibitory characteristics. Only catechins with a galloyl substituent at the 3-position showed measurable inhibition. K ic values were lower for theaflavins than catechins, with the lowest value for theaflavin-3, 3'-digallate. The lower K ic than the uncompetitive inhibition constant for the mixed-type inhibitors suggests that they bind more tightly with free PPA than with the PPA-starch complex. A 3 and/or 3'-galloyl moiety in catechin and theaflavin structures was consistently found to increase inhibition of PPA through enhanced association with the enzyme active site. A higher quenching effect of polyphenols corresponded to a stronger inhibitory activity against PPA. The red-shift of maximum emission wavelength of PPA bound with some polyphenols indicated a potential IV

show abstract

Interactions of different polyphenols with bovine serum albumin using fluorescence quenching and molecular docking

Cited by 227 publications

References 32 publications

A Correlative Multi-Spectroscopy and Docking Study for the Modeling of Drug (Luteolin and Quercetin) Binding to Bovine Serum Albumin– A Tool for the Determination of Binding Characteristics to Receptor Proteins

A Correlative Multi-Spectroscopy and Docking Study for the Modeling of Drug (Luteolin and Quercetin) Binding to Bovine Serum Albumin– A Tool for the Determination of Binding Characteristics to Receptor Proteins

Contribution of linoleic acid to the formation of advanced glycation end products in model systems during heat treatment

Studying the interactions between tea polyphenols and α-amylase

Contact Info

Product

Resources

About