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Structure-Activity Relationship of the N-terminal Helix Analog of Papiliocin, PapN

  • Jeon, Dasom (Department of Bioscience and Biotechnology, Konkuk University) ;
  • Jeong, Min-Cheol (Department of Bioscience and Biotechnology, Konkuk University) ;
  • Kim, Jin-Kyoung (Department of Bioscience and Biotechnology, Konkuk University) ;
  • Jeong, Ki-Woong (Department of Bioscience and Biotechnology, Konkuk University) ;
  • Ko, Yoon-Joo (National Center for Inter-University Research Facilities, Seoul National University) ;
  • Kim, Yangmee (Department of Bioscience and Biotechnology, Konkuk University)
  • 투고 : 2015.08.10
  • 심사 : 2015.09.25
  • 발행 : 2015.10.10

초록

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 $Lys^3$ to $Ala^{22}$, 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 ${\alpha}$-helical structure from $Lys^3$ to $Lys^{21}$. 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.

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참고문헌

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