期刊
BIOPHYSICAL JOURNAL
卷 103, 期 8, 页码 1735-1743出版社
CELL PRESS
DOI: 10.1016/j.bpj.2012.09.010
关键词
-
类别
资金
- Ministry of Culture, Sports, Science and Technology of Japan [21017002, 22500272, 22770101]
- Suntory Foundation for Life Sciences
- Grants-in-Aid for Scientific Research [22500272, 22770101, 21017002, 24570127, 22570126] Funding Source: KAKEN
Bovine lactoferrampin (LFampinB) is a newly discovered antimicrobial peptide found in the N1-domain of bovine lactoferrin (268-284), and consists of 17 amino-acid residues. It is important to determine the orientation and structure of LFampinB in bacterial membranes to reveal the antimicrobial mechanism. We therefore performed C-13 and P-31 NMR, C-13-P-31 rotational echo double resonance (REDOR), potassium ion-selective electrode, and quartz-crystal microbalance measurements for LFampinB with mimetic bacterial membrane and molecular-dynamics simulation in acidic membrane. P-31 NMR results indicated that LFampinB caused a defect in mimetic bacterial membranes. Ion-selective electrode measurements showed that ion leakage occurred for the mimetic bacterial membrane containing cardiolipin. Quartz-crystal microbalance measurements revealed that LFampinB had greater affinity to acidic phospholipids than that to neutral phospholipids. C-13 DD-MAS and static NMR spectra showed that LFampinB formed an alpha-helix in the N-terminus region and tilted 45 degrees to the bilayer normal. REDOR dephasing patterns between carbonyl carbon nucleus in LFampinB and phosphorus nuclei in lipid phosphate groups were measured by C-13-P-31 REDOR and the results revealed that LFampinB is located in the interfacial region of the membrane. Molecular-dynamics simulation showed the tilt angle to be 42 degrees and the rotation angle to be 92.5 degrees for Leu(3), which are in excellent agreement with the experimental values.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据