Interaction of Polyphenols with Proteins: Binding of (-)-Epigallocatechin Gallate to Serum Albumin, Estimated by Induced Circular Dichroism

Nozaki, Atsuo; Hori, Mami; Kimura, Toshikiro; Ito, Hideyuki; Hatano, Tsutomu

doi:10.1248/cpb.57.224

Cited by 54 publications

(37 citation statements)

References 19 publications

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“…It has been believed that flavonoids bind to the hydrophobic pockets on site I of HSA. Nozaki et al reported that EGCg was located on sites I and II of HSA (22). Taken together, this suggests that the affinity of tea catechins for HSA is influenced by their hydrophobicity, derived from the galloyl moiety.…”

Section: Discussionmentioning

confidence: 93%

“…Previous research has indicated that catechins form complexes with human serum albumin (HSA), and differences in binding affinity toward HSA are believed to determine their bioavailability. Several reports using spectrofluorometry, circular dichroism, and capillary electrophoresis have indicated that green tea catechins bind to HSA (12)(13)(14). Recently, we revealed that EGCg non-covalently binds to HSA after incubation of human serum with EGCg ( 15 ).…”

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confidence: 85%

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Influence of the Galloyl Moiety in Tea Catechins on Binding Affinity for Human Serum Albumin

Minoda

Ichikawa

Katsumata

et al. 2010

J Nutr Sci Vitaminol

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SummaryThe major catechins of green tea extract are ( Ϫ )-epicatechin (EC), ( Ϫ )-epigallocatechin (EGC), ( Ϫ )-epicatechin gallate (ECg), and ( Ϫ )-epigallocatechin gallate (EGCg). Recent research has indicated that catechins form complexes with human serum albumin (HSA) in blood, and differences in their binding affinity toward HSA are believed to modulate their bioavailability. In this study, we kinetically investigated the interaction between the catechins and HSA immobilized on a quartz-crystal microbalance (QCM). The association constants obtained from the frequency changes of QCM revealed interactions of ECg and EGCg with HSA that are 100 times stronger than those of EC and EGC. Furthermore, comparisons of these catechins by native-gel electrophoresis/blotting with redox-cycling staining revealed that, in a phosphate buffer, ECg and EGCg have a higher binding affinity toward HSA than EC and EGC. These observations indicate that catechins with a galloyl moiety have higher binding affinities toward HSA than catechins lacking a galloyl moiety.

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Section: Discussionmentioning

confidence: 93%

mentioning

confidence: 85%

Influence of the Galloyl Moiety in Tea Catechins on Binding Affinity for Human Serum Albumin

Minoda

Ichikawa

Katsumata

et al. 2010

J Nutr Sci Vitaminol

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“…3,4) We previously reported that EGCG binds to human serum albumin (HSA). 5) In the previous report, we noted the utility of circular dichroism (CD) spectra to clarify the binding of polyphenols with HSA, including the binding sites on HSA in relation to the competition with drugs having specific binding sites on the protein. EGCG has been shown to bind to sites I and II in HSA.…”

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confidence: 99%

“…The results suggested the possibility of a drug interaction concerning competition. 5) The metabolic fates of plant polyphenols have been investigated in many studies. Proanthocyanidins and catechins yield phenolic acids such as protocatechuic acid, 6) and methylation of phenolic acids, attributable to the enzyme catechol-O-methyl transferase (COMT), is also an important metabolic process of those phenolic compounds.…”

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confidence: 99%

“…The apparent binding constant (K) for each combination of drug-HSA was calculated from this relationship. 5) In the presence of a polyphenolic additive (A), the equation for the double-reciprocal plots is expressed to be where KЈ represents the apparent binding constant in the presence of the drug and the polyphenolic additive, and corresponds to where A f and K A respectively represent the molar concentration of the polyphenol unbound and the binding constant of the polyphenol on the site of HSA, on the assumption of the competitive relationship between the drug and the polyphenol. Thus, K A was estimated based on the equation…”

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confidence: 99%

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Interaction of Polyphenolic Metabolites with Human Serum Albumin: A Circular Dichroism Study

Nozaki

Kimura

Ito

et al. 2009

CHEMICAL & PHARMACEUTICAL BULLETIN

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Plant‐Inspired Pyrogallol‐Containing Functional Materials

Shin

Park

Lee

2019

Adv Funct Materials

152

106

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Pyrogallol-containing molecules are ubiquitous in the plant kingdom. The chemical synthesis of these molecules remains challenging. Thus, they are obtained via purification from heterogeneous mixtures of plant extracts. Previous studies have focused on their biological roles, such as antioxidants. Additionally, the molecules are used as ink colorants and in tanning processes for leather. Recently, many disciplines have paid attention to adhesiveness of pyrogallol-containing molecules, including the control of interface properties in energy storage/generation and medical devices, as well as the changes in wettability related to membrane technologies. In particular, pyrogallol-containing molecules act as "molecular glues," binding to virtually all biomacromolecules, for example, DNA/RNA, soluble proteins, insoluble extracellular matrices, and peptides. Furthermore, the cohesion of pyrogallol by forming pyrogallol-to-pyrogallol covalent bonds is useful for the preparation of bulk hydrogels and thin films. The content of this review focuses on interactions with biomacromolecules used as molecular glues, used as modifiers in material-independent surface chemistry, and applied as chemical moieties to form covalent linkages to fabricate hydrogels and related biomaterials. Future perspectives include the development of new pyrogallol-containing materials, the understanding of chirality in adhesion, and the improvement of the mechanical stability for applications in various biomedical, energy, and industrial devices. molecules, strategies for surface modifications, and biomedical applications (Figure 1). Based on the timeline of pyrogallol research, we begin by describing the basic physicochemical properties of pyrogallol analogs, focusing on intermolecular interactions with macromolecules. Section 2 introduces the chemical versatility of pyrogallol analogs in macromolecular complexation, and analytical methods for the complexation are explained. Furthermore, the biological functions of pyrogallol analogs, particularly their therapeutic effects on cancers and inflammatory diseases, are explained. Next, surface modification strategies using pyrogallol-containing molecules are explained (Section 3). We discuss pyrogallol-derived formulations for biomedical purposes, ranging from hydrogels to particles (Section 4). Finally, we conclude with an outlook for the further development and implementation of natural pyrogallol analogs and pyrogallol-conjugated synthetic polymers. This review will be helpful for understanding past studies and current progress in pyrogallol-containing molecules research and for predicting future perspectives. Chemical and Structural Analysis of Colloidal ComplexationEarly uses largely involved intermolecular interactions between pyrogallol analogs and proteins. Pyrogallol analog complexations were particularly effective in studies of proline-rich proteins (PRPs)

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Interaction of Polyphenols with Proteins: Binding of (-)-Epigallocatechin Gallate to Serum Albumin, Estimated by Induced Circular Dichroism

Abstract: The binding of (؊)-epigallocatechin gallate (EGCG), a representative natural polyphenol, to human serum albumin (HSA) and bovine serum albumin (BSA) was investigated using induced circular dichroism (

Cited by 54 publications

References 19 publications

Influence of the Galloyl Moiety in Tea Catechins on Binding Affinity for Human Serum Albumin

Influence of the Galloyl Moiety in Tea Catechins on Binding Affinity for Human Serum Albumin

Interaction of Polyphenolic Metabolites with Human Serum Albumin: A Circular Dichroism Study

Plant‐Inspired Pyrogallol‐Containing Functional Materials

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