Goo, HC Hwang, YS Choi, YR Cho, HN Suh, H 2024-01-21T08:02:04Z 2024-01-21T08:02:04Z 2021-09-03 2003-12 0142-9612 https://pubs.kist.re.kr/handle/201004/138063 Collagen is regarded as one of the most useful biomaterials. The excellent biocompatibility and safety due to its biological characteristics, such as biodegradability and weak antigenecity, made collagen the primary source in biomedical application. Collagen has been widely used in the crosslinked form to extend the durability of collagen. The chemical treatment influences the structural integrity of collagen molecule resulting in the loss of triple helical characteristic. The structural characteristic of collagen is importantly related to its biological function for the interaction with cell. In this study, structural stability of collagen was enhanced thought EGCG treatment, resulting in high resistance against degradation by bacterial collagenase and MMP-1, which is confirmed by collagen zymography. The triple helical structure of EGCG-treated collagen could be maintained at 37degreesC in comparison with collagen, which confirmed by CD spectra analysis, and EGCG-treated collagen showed high free-radical scavenging activity. Also, with fibroblasts culture on EGCG-treated collagen, the structural stability of EGCG-treated collagen provided a favorable support for cell function in cell adhesion and actin filament expression. These observations underscore the need for native, triple helical collagen conformation as a prerequisite for integrin-mediated cell adhesion and functions. According to this experiment, EGCG-treated collagen assumes to provide a practical benefit to resist the degradation by collagenase retaining its structural characteristic, and can be a suitable biomaterial for biomedical application. (C) 2003 Elsevier Ltd. All rights reserved. English ELSEVIER SCI LTD ALPHA-1 BETA-1 I COLLAGEN MATRIX EXPRESSION CLEAVAGE ADHESION TISSUE OZONE TEA STABILIZATION Development of collagenase-resistant collagen and its interaction with adult human dermal fibroblasts Article 10.1016/S0142-9612(03)00431-9 1 BIOMATERIALS, v.24, no.28, pp.5099 - 5113 BIOMATERIALS 24 28 5099 5113 scie scopus 000186674000004 2-s2.0-0142057078 Engineering, Biomedical Materials Science, Biomaterials Engineering Materials Science Article ALPHA-1 BETA-1 I COLLAGEN MATRIX EXPRESSION CLEAVAGE ADHESION TISSUE OZONE TEA STABILIZATION EGCG collagen collagenase resistance structural stability free-radical scavenging activity cell adhesion actin filament