| Title: | Lipopolysaccharide-bound structure of the antimicrobial peptide cecropin P1 determined by nuclear magnetic resonance spectroscopy |
| Authors: | Baek, Mi-Hwa Browse this author |
| Kamiya, Masakatsu Browse this author →KAKEN DB |
| Kushibiki, Takahiro Browse this author |
| Nakazumi, Taichi Browse this author |
| Tomisawa, Satoshi Browse this author |
| Abe, Chiharu Browse this author |
| Kumaki, Yasuhiro Browse this author |
| Kikukawa, Takashi Browse this author →KAKEN DB |
| Demura, Makoto Browse this author →KAKEN DB |
| Kawano, Keiichi Browse this author →KAKEN DB |
| Aizawa, Tomoyasu Browse this author →KAKEN DB |
| Keywords: | antimicrobial peptide |
| cecropin P1 |
| lipopolysaccharide |
| nuclear magnetic resonance |
| transferred nuclear Overhauser effect |
| Issue Date: | Apr-2016 |
| Publisher: | Wiley-Blackwell |
| Journal Title: | Journal of peptide science |
| Volume: | 22 |
| Issue: | 4 |
| Start Page: | 214 |
| End Page: | 221 |
| Publisher DOI: | 10.1002/psc.2865 |
| PMID: | 26939541 |
| Abstract: | Antimicrobial peptides (AMPs) are components of the innate immune system and may be potential alternatives to conventional antibiotics because they exhibit broad-spectrum antimicrobial activity. The AMP cecropin P1 (CP1), isolated from nematodes found in the stomachs of pigs, is known to exhibit antimicrobial activity against Gram-negative bacteria. In this study, we investigated the interaction between CP1 and lipopolysaccharide (LPS), which is the main component of the outer membrane of Gram-negative bacteria, using circular dichroism (CD) and nuclear magnetic resonance (NMR). CD results showed that CP1 formed an -helical structure in a solution containing LPS. For NMR experiments, we expressed N-15-labeled and C-13-labeled CP1 in bacterial cells and successfully assigned almost all backbone and side-chain proton resonance peaks of CP1 in water for transferred nuclear Overhauser effect (Tr-NOE) experiments in LPS. We performed N-15-edited and C-13-edited Tr-NOE spectroscopy for CP1 bound to LPS. Tr-NOE peaks were observed at the only C-terminal region of CP1 in LPS. The results of structure calculation indicated that the C-terminal region (Lys15-Gly29) formed the well-defined -helical structure in LPS. Finally, the docking study revealed that Lys15/Lys16 interacted with phosphate at glucosamine I via an electrostatic interaction and that Ile22/Ile26 was in close proximity with the acyl chain of lipid A. Copyright (c) 2016 European Peptide Society and John Wiley & Sons, Ltd. |
| Type: | article (author version) |
| URI: | http://hdl.handle.net/2115/64933 |
| Appears in Collections: | 理学院・理学研究院 (Graduate School of Science / Faculty of Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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