Faculty of Pharmaceutical Sciences, University of British Columbia, Vancouver, BC, V6T 1Z3, Canada.
J Mater Sci Mater Med. 2010 May;21(5):1435-43. doi: 10.1007/s10856-010-4019-3. Epub 2010 Feb 17.
Collagen based cosmetic fillers require repeat treatments due to collagenase derived degradation of the filler in the intradermal injection site. The objective of this study was to investigate the inhibition of this degradation by the galloyl-containing compounds tannic acid, epigallocatechin gallate (EGCG), epicatechin gallate (ECG) and gallic acid (GA). A gel permeation chromatography assay was developed to quantitate the collagenase induced reductions in collagen molecular weight. The binding of the compounds to collagen was measured using HPLC. The stabilization of collagen was measured using Differential Scanning Calorimetry (DSC). Tannic acid, EGCG and ECG (but not GA) were found to strongly inhibit collagen degradation at concentrations in the low micromolar range. The compounds bound strongly to collagen and stabilized collagen. It is concluded that tannic acid, EGCG and ECG bind to collagen via extensive hydrogen bonding augmented by some hydrophobic interactions and prevent the free access of collagenase to active sites on the collagen chains.
基于胶原蛋白的美容填充物由于在真皮注射部位的胶原蛋白酶降解，需要重复治疗。本研究的目的是研究含没食子酰基的化合物单宁酸、表没食子儿茶素没食子酸酯 (EGCG)、表儿茶素没食子酸酯 (ECG) 和没食子酸 (GA) 对这种降解的抑制作用。开发了凝胶渗透色谱法测定胶原酶诱导的胶原分子量降低。使用 HPLC 测量化合物与胶原的结合。使用差示扫描量热法 (DSC) 测量胶原的稳定性。发现单宁酸、EGCG 和 ECG（但不是 GA）在低微摩尔浓度范围内可强烈抑制胶原降解。这些化合物与胶原蛋白强烈结合并稳定胶原蛋白。结论是，单宁酸、EGCG 和 ECG 通过广泛的氢键与胶原蛋白结合，辅之以一些疏水相互作用，从而阻止胶原蛋白酶自由进入胶原蛋白链上的活性位点。
