Probing the binding of (+)-catechin to bovine serum albumin by isothermal titration calorimetry and spectroscopic techniques

Li, Xiangrong; Hao, Yongbing

doi:10.1016/j.molstruc.2015.02.082

Cited by 28 publications

(18 citation statements)

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“…Catechins are plant polyphenolic compounds belonging to a subclass, known as flavan-3-ols, in the flavonoid family. It is well known that the number of galloyl and hydroxyl groups in the molecular structure of catechins plays an important role in their biological activities (Yuksel et al, 2010;Li & Hao, 2015). (À)-Epicatechin (EC), (À)-epigallocatechin (EGC), (À)-epigallocatechin gallate (EGCG) and (À)-epicatechin gallate (ECG) are the major green tea catechins (Wu et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

Interactions of digestive enzymes and milk proteins with tea catechins at gastric and intestinal pH

Чан

Chen

et al. 2016

Int J of Food Sci Tech

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Summary The interactions of digestive enzymes (pepsin, pancreatin) and milk proteins (β‐casein, β‐lactoglobulin (β‐Lg)) with (−)‐epigallocatechin gallate (EGCG), (−)‐epigallocatechin (EGC) and (−)‐epicatechin (EC) at gastric and intestinal pH were investigated by fluorescence spectroscopy. The results indicated that in the gastric environment, all three tea catechins showed binding affinities in descending order of strength with β‐casein first, followed by β‐Lg and then pepsin. The highest affinity was observed for EGCG–β‐casein, with a binding constant (KA) of 2.502(±0.201) × 105 m−1. In the intestinal environment, the binding strengths of the proteins with EGCG and EGC were in the order β‐Lg > pancreatin > β‐casein; for binding with EC, the strength order was β‐casein > β‐Lg > pancreatin. The combination EGCG–β‐Lg had the strongest binding affinity, with a KA of 14.300(±0.997) × 105 m−1. Thermodynamic analysis revealed that tea catechins complexed with milk proteins and digestive enzymes via different hydrophilic and hydrophobic interactions depending on the different digestion environments and types of catechins, proteins and enzymes.

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Section: Introductionmentioning

confidence: 99%

Interactions of digestive enzymes and milk proteins with tea catechins at gastric and intestinal pH

Чан

Chen

et al. 2016

Int J of Food Sci Tech

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“…31 Ross and Subramanian 33 have characterized the sign of the thermodynamic parameters with various kinds of interaction which may take place in the protein association process. 34 Table 1 shows that ΔH° and ΔS° values are negative and positive, respectively, for HSA:BZL, HSA:MTZ and HSA:MZ, indicating hydrogen bonding and electrostatic forces as the main binding forces in the binding process. 35 While for HSA:NFX interaction, hydrogen bonding and hydrophobic interaction are the main binding forces.…”

Section: Resultsmentioning

confidence: 99%

“…33 From the standpoint of water structure, positive entropy is often regarded as a typical signature of hydrophobic interaction, since the water molecules which are arranged in an orderly fashion around the ligand and the protein molecules acquire a more random configuration as a result of hydrophobic interactions. 34 Other possible sources for entropic contributions like residual flexibility of ligand and/or the protein binding site can also be considered. The negative enthalpy value may be explained when small molecules are partially inserted into a hydrophobic cavity of HSA formed by folding and twisting of the peptide chain.…”

Section: Resultsmentioning

confidence: 99%

“…In the present case, the hydrophobic interaction between the antiparasitc drugs and the cavity would cause an exothermic process. 34,36 Note that BZL, MTZ and MZ structures present similar structural characteristics, with just one (nitro) group with high electron density and H-donors and/or aromatic groups connected to an imidazole ring, while the NFX structure is more linear, and has the nitro group in one end (furan, not imidazole), and a second (sulfone) group with high electron density, at the other extremity, with no aromatic group or H-donor in between (Figure 1). In aqueous phase, NFX coordinates with a large number of solvent molecules, using its H-acceptor sites; when NFX penetrates the protein cavity, which is relatively hydrophobic, these molecules are liberated, and the bulk volume previously occupied by NFX is also taken by water; furthermore, water molecules which occupied the protein cavity, are expelled to the external space, where they enjoy the increased degrees of freedom.…”

Section: Resultsmentioning

confidence: 99%

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Multiple Spectroscopic and Theoretical Approaches to Study the Interaction between HSA and the Antiparasitic Drugs: Benznidazole, Metronidazole, Nifurtimox and Megazol

Chaves¹,

Ferreira²,

Silva³

et al. 2018

J. Braz. Chem. Soc.

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The interaction between four antiparasitic drugs (benznidazole (BZL), metronidazole (MTZ), nifurtimox (NFX) and megazol (MZ)) with human serum albumin (HSA), the main vehicle of biodistribution of xenobiotics, hydrophobic, small and endogenous molecules in the bloodstream, was evaluated by multiple spectroscopic techniques and theoretical calculations. In all cases quenching of the fluorescence of HSA by these drugs involve a static mechanism, due to ground state association. There is just one main binding site in HSA for these four ligands (Sudlow's site I); binding is spontaneous, moderate, does not have any effect on the polarity around the Tyr and Trp residues and does not perturb significantly the secondary structure of the protein. Molecular docking studies suggest hydrogen bonding and hydrophobic interactions as the main binding forces, i.e., BZL associates with the Trp-214 residue via hydrophobic interactions and with Gln-220, Arg-221 and Glu-449 residues via hydrogen bonding; whereas MTZ associates with Leu-197 and Leu-480 residues via hydrophobic interactions and with Trp-214, Glu-449 and Ser-453 via hydrogen bonding. Furthermore, electrostatic interactions were also suggested for HSA:MZ and HSA:NFX.

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“…Catechin ( Figure 1) is a natural flavonoid and one of the principal active components of green tea, which possesses strong antioxidant, antiinflammatory, neuroprotective and anticancer activities and so on [1][2][3]. Therefore, catechin is emerging as a promising bioactive ingredient with potential applications in functional foods and medicines.…”

Section: Introductionmentioning

confidence: 99%

Physicochemical Characterization of Inclusion Complex of Catechin and Glucosyl-β-Cyclodextrin

Li¹,

Zhang²,

Ma³

2016

Trop. J. Pharm Res

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Purpose: To investigate the suitability of glucosyl-β-cyclodextrin (G-β-CD) to form inclusion complex with catechin, and characterize the physicochemical properties of the inclusion complex of catechin and G-β-CD. Methods: Catechin and G-β-CD was mixed in water at the same molar ratio, stirred at 20 °C for 48 h and lyophilized to obtain the complex. Its physicochemical properties were investigated by ultravioletvisible spectrometry (UV), Fourier transform infrared spectroscopy (FT-IR), scanning electron microscopy (SEM), X-ray diffractometry (XRD) and differential scanning calorimetry (DSC

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Probing the binding of (+)-catechin to bovine serum albumin by isothermal titration calorimetry and spectroscopic techniques

Cited by 28 publications

References 68 publications

Interactions of digestive enzymes and milk proteins with tea catechins at gastric and intestinal pH

Interactions of digestive enzymes and milk proteins with tea catechins at gastric and intestinal pH

Multiple Spectroscopic and Theoretical Approaches to Study the Interaction between HSA and the Antiparasitic Drugs: Benznidazole, Metronidazole, Nifurtimox and Megazol

Physicochemical Characterization of Inclusion Complex of Catechin and Glucosyl-β-Cyclodextrin

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