Yamauchi Kosei, Soyano Mayu, Kobayashi Miho, Kamatari Yuji O, Mitsunaga Tohru
Faculty of Applied Biological Sciences, Gifu University, Gifu, Gifu 501-1193, Japan.
Graduate School of Natural Science and Technology, Gifu University, 1-1 Yanagido 501-1193 Gifu, Japan.
Food Chem. 2023 Aug 1;416:135870. doi: 10.1016/j.foodchem.2023.135870. Epub 2023 Mar 6.
Tannins are involved in the taste of foods and multi bioactivity of traditional herbal medicines. The characteristics of tannins are believed to derive from their connectivity with proteins. However, the mode of interaction between proteins and tannins is not yet understood because of the complexity of the tannin structure. Then this study aimed to elucidate the detail binding mode of tannin and protein by the H-N HSQC NMR method using the N-labeled MMP-1that have not been used so far. The HSQC results suggested cross-link sites between MMP-1s, which cause protein aggregation and inhibit MMP-1 activity. This study presents the first 3D protein aggregation model of condensed tannins, which is important for understanding the bioactivity of polyphenols. Furthermore, it can broaden the understanding of the range of interactions between other proteins and polyphenols.
单宁参与食物的味道以及传统草药的多种生物活性。人们认为单宁的特性源于它们与蛋白质的结合。然而，由于单宁结构的复杂性，蛋白质与单宁之间的相互作用模式尚未明确。因此，本研究旨在通过使用迄今尚未使用过的N标记的基质金属蛋白酶-1（MMP-1），采用H-N HSQC核磁共振方法阐明单宁与蛋白质的详细结合模式。HSQC结果表明MMP-1之间存在交联位点，这会导致蛋白质聚集并抑制MMP-1活性。本研究提出了缩合单宁的首个三维蛋白质聚集模型，这对于理解多酚的生物活性很重要。此外，它可以拓宽对其他蛋白质与多酚之间相互作用范围的理解。
