Journal
JOURNAL OF ANALYTICAL SCIENCE AND TECHNOLOGY
Volume 11, Issue 1, Pages -Publisher
SPRINGER INTERNATIONAL PUBLISHING AG
DOI: 10.1186/s40543-020-00213-x
Keywords
Antimicrobial peptide; Bactericidal; Cosmetic preservatives; LL-37; NMR structure
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Funding
- Basic Science Research Program through the National Research Foundation of Korea (NRF) - Ministry of Education, Science, and Technology of Korea [NRF-2018R1D1A1B07043540, NRF-2018R1C1B5085101]
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KR-12 was derived from the human antimicrobial peptide, LL-37. KR-12 maintains the antimicrobial activity of LL-37 and has low toxicity against human cells, thereby showing a high potential for various applications. In this study, the three-dimensional structure of KR-12 analog (KR-12-pa) was determined by solution NMR spectroscopy. The NMR structure of KR-12-pa revealed a nearly perfect amphipathic alpha-helical structure composed of multiple hydrophobic and positively charged residues. The minimal inhibitory concentration of KR-12-pa for various bacterial and yeast cells suggested that KR-12-pa has a much stronger antimicrobial activity than commercial cosmetic preservatives. In addition, KR-12-pa in cosmetic formulations showed much stronger bactericidal effects than conventional cosmetic preservatives and very low cytotoxicity to mammalian cells. These results suggest that KR-12-pa is applicable as a cosmetic preservative.
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