논문 (학술지)
Isolation and structural elucidation of pelgipeptin E, a novel pore-forming pelgipeptin analog from Paenibacillus elgii with low hemolytic activity
등록번호 | RPMS-2019-0190815990 | SCI 구분
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※구분 : SCI(SCIE포함), 비SCI |
SCI |
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저자명 (주·공동저자) | Kim Jueun; Il Kim Pyoung; Bong Ki Moon; Il Kim Jae; Shin Song Yub; Song Jaekyeong; Min Hye Jung; Lee Chul Won | ||
논문구분 | 국외전문학술지 | 학술지명 | JOURNAL OF ANTIBIOTICS |
ISSN | 0021-8820 | 학술지 출판일자 | 2018-12-01 |
학술지 볼륨번호 | 71 | 논문페이지 | 1008 ~ 1017 |
학술지 임팩트팩터 | 2.237 | 기여율 | 100 % |
DOI | 10.1038/s41429-018-0095-2 | ||
초록 | Pelgipeptins are cyclic lipopeptides composed of nine amino acids and a short fatty acid chain. In the present study, we report a novel pelgipeptin peptide that was isolated from Paenibacillus elgii BC34-6 and named pelgipeptin E (PGP-E). The molecular mass of PGP-E was 1072 Da as determined by liquid chromatography-mass spectrometry and the amino acid sequence was elucidated by tandem mass spectrometry. The complete molecular structure of PGP-E was characterized using 2D NMR spectroscopy. PGP-E consisted of a cyclic peptide backbone of Dab1-Val2-Dab3-Phe4-Leu5-Dab6-Val7-Leu8-Ser9 and a lipid chain (-CH2CH2CH3). PGP-E had broad antimicrobial activity against gram-negative and -positive bacteria, including methicillin-resistant Staphylococcus aureus strains. Furthermore, the mode of action of PGP-E was investigated using calcein dye leakage and membrane depolarization assays, which suggest that PGP-E acts via a membrane-active mechanism. The hemolytic activity of PGP-E was significantly lower than that of melittin, a well-known membrane-active peptide derived from bee venom. These results suggest that PGP-E is a potential candidate in the development of new peptide antibiotics. |
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