HUSCAP logo Hokkaido Univ. logo

Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Science / Faculty of Science >
Peer-reviewed Journal Articles, etc >

Lipopolysaccharide-bound structure of the antimicrobial peptide cecropin P1 determined by nuclear magnetic resonance spectroscopy

Files in This Item:
manuscript_160103.pdf128.81 kBPDFView/Open
Please use this identifier to cite or link to this item:

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
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)
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)

Submitter: 相沢 智康

Export metadata:

OAI-PMH ( junii2 , jpcoar )

MathJax is now OFF:


Feedback - Hokkaido University