DOI QR코드

DOI QR Code

Study on Effect of Skin Elasticity by Polar Low Molecular Weight Keratin Peptide

극성 저분자 케라틴 펩타이드에 의한 피부 탄력 변화 연구

  • 맹지혜 ((주)씨알에이코리아) ;
  • 남개원 (서원대학교 바이오코스메틱학과)
  • Received : 2020.06.12
  • Accepted : 2020.08.06
  • Published : 2020.09.30

Abstract

Using Fervidobacterium islandicum AW-1, polar low molecular weight keratin peptides were produced and confirmed through factors related to the skin elasticity. As a result of confirming the cytotoxicity and collagen synthesis ability according to the concentration of the polar low molecular weight keratin peptide in human fibroblasts, it was confirmed that the cytotoxicity did not appear and the collagen synthesis in human fibroblasts was increased. A mask pack containing a polar low-molecular weight keratin peptide was used, and a test product was used for 4 weeks in 22 healthy women subjects. As a result, it showed statistically significant effects on skin elasticity, skin torsion elasticity, skin color and moisture improvement. Through this test, it was confirmed that the polar low-molecular keratin peptide can be used as a cosmetic ingredient that helps improve skin elasticity.

본 연구에서는 Fervidobacterium islandicum AW-1를 이용하여 극성 저분자 케라틴 펩타이드를 생산하고, 피부 탄력과 관련한 인자를 확인하여, 화장품 원료로서 극성 저분자 케라틴 펩타이드의 가능성을 확인하였다. 인체섬유아세포에 극성 저분자 케라틴 펩타이드를 농도에 따라 세포독성 및 콜라겐 합성능을 확인한 결과, 세포 독성은 나타나지 않았고, 인체섬유아세포 내 콜라겐 합성을 증가시키는 것을 확인하였다. 극성 저분자 케라틴 펩타이드를 함유한 마스크팩을 만들어, 22 명의 건강한 성인 피험자를 대상으로 4 주 동안 시험제품을 사용한 결과, 피부 탄력 및 피부 비틀림 탄력 개선, 수분량 증가, 피부색 개선에서 통계적으로 유의한 효과를 나타냈다. 이를 통해 극성 저분자 케라틴 펩타이드는 피부 탄력 개선에 도움을 주는 화장품 원료로 사용할 수 있음을 확인하였다.

Keywords

References

  1. N. J. Gang, H. S. Jin, S. E. Lee, H. J. Kim, and H. Koh, New approaches towards the discovery and evaluation of bioactive peptides from natural resources, Critical Reviews in Environmental Science and Technology, 50(1), 72 (2019).
  2. T. Uhlig, T. Kyprianou, F. G. Matinelli, C. A. Oppici, D. Heiligers, D. Hills, X. R. Calvo, and P. Verhaert, The emergence of peptides in the pharmaceutical business: From exploration to exploitation, EuPA Open Proteomics. 4, 58 (2014). https://doi.org/10.1016/j.euprot.2014.05.003
  3. H. Korhonen and A. Pihlanto, Food-derived bioactive peptides-opportunities for designing future foods, Curr. Pharm. Des., 9(16), 1297 (2003). https://doi.org/10.2174/1381612033454892
  4. G. Tucker. B. DeSilva, J. Dressman, M. Ito, T. Kumamoto, D. Mager, H. Mahler, A. H. M. Zeem G. M. Pauletti, H. Sasaki, V. Shah, D. Tang, and M. Ward, Current challenges and potential opportunities for the pharmaceutical sciences to make global impact: An FIP perspective, J Pharm Sci, 105(9), 2489 (2016). https://doi.org/10.1016/j.xphs.2015.12.001
  5. B. Wang, W. Yang, J. McKittrick, and M. A. Meyers, Keratin: Structure, mechanical properties, occurrence in biological organisms, and efforts at bioinspiration, Progress in Materials Science. 76, 229 (2016). https://doi.org/10.1016/j.pmatsci.2015.06.001
  6. J. Henry, E. Toulza, C. Y. Hsu, L. Pellerin, S. Balica, J. Mazereeuw-Hautier, C. Paul, G. Serre., N. Jonca, and M. Simon, Update on the epidermal differentiation complex, Front Biosci (Landmark Ed), 17, 1517 (2012). https://doi.org/10.2741/4001
  7. Y. J. Lee, H. Jeong, G. S. Park, Y. Kwak, S. J. Lee, M. K. Park, J. Y. Kim, H. K. Kang, J. H. Shin, and D. W. Lee, Genome sequence of a native-feather degrading extremely thermophilic Eubacterium, Fervidobacterium islandicum AW-1, Stand Genomic Sci, 10, 71 (2015). https://doi.org/10.1186/s40793-015-0063-4
  8. H. S. Jin, K. Song, J. H. Baek, J. E. Lee, D. J. Kim, G. W. Nam, N. J. Kang, and D. W. Lee, Identification of matrix metalloproteinase-1-suppressive peptides in feather keratin hydrolysate, J. Agric. Food Chem., 66(48), 12719 (2018). https://doi.org/10.1021/acs.jafc.8b05213
  9. G. W. Nam, D. W. Lee, H. S. Lee, N. J. Lee, B. C. Kim, E. A. Choe, J. K. Hwang, M. T. Suhartono, and Y. R. Pyun, Native-feather degradation by Fervidobacterium islandicum AW-1, a n ewly isolated keratinase-producing thermophilic anaerobe, Arch. Microbiol., 178(6), 538 (2002). https://doi.org/10.1007/s00203-002-0489-0
  10. H. S. Jin, S. Y. Park, K. Kim, Y. J. Lee, G. W. Nam, N. J. Kang, and D. W. Lee, Development of a keratinase activity assay using recombinant chicken feather keratin substrates, PLoS ONE, 12(2), e0172712 (2017). https://doi.org/10.1371/journal.pone.0172712
  11. Y. J. Lee, I. Dganasingh, J. S. Ahn, H. S. Jin, J. M. Choi, S. H. Lee, and D. W. Lee, Biochemical and structural characterization of a keratin-degrading M32 carboxypeptidase from Fervidobacterium islandicum AW-1, Biochem. Biophys. Res. Commun., 468(4), 927 (2015). https://doi.org/10.1016/j.bbrc.2015.11.058
  12. G. W. Nam, Study on changes of hair and scalp characteristics by keratin peptides, J. Soc. Cosmet. Sci. Korea, 45(4), 353 (2019). https://doi.org/10.15230/SCSK.2019.45.4.353