In Young Bae, Yoo Kyung Han, Hyun Jeong Je, Hyun Jun Lee, Hyeon Gyu Lee
언어
영어(ENG)
URL
https://www.earticle.net/Article/A375630
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원문정보
초록
영어
An anti-aging peptide was prepared from fish collagen hydrolysate (FCH) by ultrafiltration (MWCO; 1 kDa) and reversed-phased high performance liquid chromatography (RP-HPLC). Its anti-aging properties were evaluated based on the procollagen-synthesizing and MMP-1-inhibiting activities in Hs68 cells. A potent anti-aging peptide (fraction I-I) increased collagen synthesis by 46% and also inhibited MMP-1 secretion by 77%, compared with unpurified FCH. The amino acid sequence of fraction I-I was identified to be Gly-Arg-Arg-Gly-Asn-Lys (GRRGNK; the repeating Gly-X-Y sequence in collagen), and it had a molecular mass of 686.175 Da. It revealed that the anti-aging activity of GRRGNK was mainly due to skin protective effects. These results demonstrated that fish collagen hydrolysate may be a potential source of anti-aging peptides, which could be utilized in various field, including foods, cosmetics, and pharmaceuticals.
한국어
본 연구에서는 어류 유래 콜라겐 가수분해물로부터 한외여과법(MWCO; 1 kDa)과 역상액체크로마토그래피를 이용하여 항노화 활성 기능성 펩타이드를 분리, 정제하고자 하였다. 펩타이드의 분리, 정제에 따른 항노화 활성 변화는 Hs68 세포를 사용하여 procollagen 합성능과 MMP-1 저해능을 측정하여 확인하였다. 콜라겐 가수분해물과 비교하 여 최종 분리, 정제된 기능성 펩타이드의 procollagen 합성과 MMP-1 저해는 각각 46%와 77% 향상되었다. 또한 기능성 펩타이드의 구조는 Gly-Arg-Arg-Gly-Asn-Lys (GRRGNK; 콜라겐의 기본 구조인 Gly-X-Y sequence와 유 사)의 서열을 보였고, 분자량은 686.175 Da으로 분석되었다. 따라서 본 연구에서는 어류 콜라겐 가수분해물로부터 분리한 펩타이드가 식품, 화장품, 의약품 등의 피부노화 지연 효과를 보이는 기능성 원료로 다양하게 사용할 수 있는 가능성을 확인하였다.
목차
Abstract 요약 1. Introduction 2. Materials and Methods 2.1 Materials 2.2 Cytotoxicity of FCHs 2.3 Procollagen synthesis assay 2.4 UV-induced collagenase inhibition assay 2.5 Ultrafiltration 2.6 Reversed-phased high performance liquid chromatography (RP-HPLC) 2.7 Amino acid composition 2.8 Molecular mass and peptide sequencing 2.9 Synthesis of the peptide 2.10 Statistical analysis 3. Results and Discussion 3.1 Cytotoxicity and anti-aging properties of FCH 3.2 Anti-aging properties of the fractions from FCH 3.3 Anti-aging properties of fractions isolated from HPLC 3.4 Identification of the anti-aging peptide 3.5 Anti-aging properties of the synthesized peptide 4. Conclusion REFERENCES