투고논문
| JKMRS Volume 19, No 2, pp 54-60; Structure-Activity Relationsh... | |
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| 2015년 10월 13일 / 조회수: 736 | |
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Structure-Activity Relationship of the
N-terminal Helix Analog of Papiliocin, PapN Dasom Jeon1, Min-Cheol Jeong1,
Jin-Kyoung Kim1, Ki-Woong Jeong1, Yoon-Joo Ko2,
and Yangmee Kim1* 1Department of Bioscience and Biotechnology,
Konkuk University, Seoul 143-701, South Korea 2National Center for Inter-University
Research Facilities, Seoul National University, Seoul 151-742, South Korea Received Aug 10, 2015; Revised
Sep 15, 2015; Accepted Sep 25, 2015
Abstract Papiliocin,
from the swallowtail butterfly, Papilio xuthus, shows high bacterial cell
selectivity against Gram-negative bacteria. Recently, we designed a 22mer
analog with N-terminal helix from Lys3 to Ala22, PapN. It
shows outstanding antimicrobial activity against Gram-negative bacteria with
low toxicity against mammalian cells. In this study, we determined the 3-D
structure of PapN in 300 mM DPC micelle using NMR spectroscopy and investigated
the interactions between PapN and DPC micelles. The results showed that PapN
has an amphipathic α-helical structure from Lys3 to Lys21. STD-NMR and DOSY experiment showed that this
helix is important in binding to the bacterial cell membrane. Furthermore, we
tested antibacterial activities of PapN in the presence of salt for therapeutic
application. PapN was calcium- and magnesium-resistant in a physiological
condition, especially against Gram-negative bacteria, implying that it can be a
potent candidate as peptide antibiotics.
Keywords Papillion, PapN, Antimicrobial
peptide, Structure, NMR
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| 첨부파일 | 1_김양미.pdf |