Interaction of polyphenols with proteins: binding of (-)-epigallocatechin gallate to serum albumin, estimated by induced circular dichroism
| Autor: | Mami Hori, Toshikiro Kimura, Akiko Nozaki, Hideyuki Ito, Tsutomu Hatano |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Circular dichroism
Digitoxin Serum albumin Epigallocatechin gallate complex mixtures Catechin chemistry.chemical_compound Tolbutamide Phenols Drug Discovery medicine Animals Humans heterocyclic compounds Binding site Bovine serum albumin Serum Albumin Flavonoids Binding Sites biology Circular Dichroism food and beverages Polyphenols Proteins Serum Albumin Bovine General Chemistry General Medicine Human serum albumin body regions chemistry Biochemistry biology.protein Cattle Indicators and Reagents sense organs medicine.drug Protein Binding |
| Zdroj: | ResearcherID |
| ISSN: | 0009-2363 |
| Popis: | 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 (CD). The site of the binding EGCG-HSA was analyzed based on the competition with drugs with known binding sites on HSA, such as phenylbutazone (PB) and diazepam (DP). Double-reciprocal plot analyses showed the competitive relations with the site-I- (PB and tolbutamide, TB) and site-II-binding drugs (DP and ibuprofen, IP) indicating the binding of EGCG to sites I and II on HSA, while digitoxin (DG), a site-III-binding drug, did not affect the binding of EGCG. In an analogous way, the competitive relations were observed between EGCG and the site-I- (PB and TB) and site-II-binding (ethacrynic acid, EA) drugs for the binding of EGCG and BSA. The site-III drug DG also showed competitive binding with EGCG to BSA. The binding of EGCG to the albumins indicated its affinity to sites I and II on HSA, while competitive binding for all three sites was observed on BSA. |
| Databáze: | OpenAIRE |
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