期刊
EUROPEAN JOURNAL OF ORAL SCIENCES
卷 120, 期 2, 页码 132-139出版社
WILEY
DOI: 10.1111/j.1600-0722.2012.00947.x
关键词
alpha-amylase; (-)-epigallocatechin gallate; salivary proteins; tea catechin
资金
- Ministry of Education, Culture, Sports, Science, and Technology, Japan [21592650]
- Grants-in-Aid for Scientific Research [21592650] Funding Source: KAKEN
Green tea is a popular drink throughout the world, and it contains various components, including the green tea polyphenol (-)-epigallocatechin gallate (EGCG). Tea interacts with saliva upon entering the mouth, so the interaction between saliva and EGCG interested us, especially with respect to EGCG-protein binding. SDS-PAGE revealed that several salivary proteins were precipitated after adding EGCG to saliva. Matrix-assisted laser desorption/ ionization time-of-flight mass spectrometry (MALDI- TOF MS) peptide mass fingerprinting indicated that the major proteins precipitated by EGCG were alpha-amylase, S100, and cystatins. Surface plasmon resonance revealed that EGCG bound to alpha-amylase at dissociation constant (K-d) = 2.74 x 10(-6) M, suggesting that EGCG interacts with salivary proteins with a relatively strong affinity. In addition, EGCG inhibited the activity of alpha-amylase by non-competitive inhibition, indicating that EGCG is effective at inhibiting the formation of fermentable carbohydrates involved in caries formation. Interestingly, alpha- amylase reduced the antimicrobial activity of EGCG against the periodontal bacterium Aggregatibacter actinomycetemcomitans. Therefore, we considered that EGCG-salivary protein interactions might have both protective and detrimental effects with respect to oral health.
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