期刊
TOXINS
卷 5, 期 4, 页码 637-664出版社
MDPI
DOI: 10.3390/toxins5040637
关键词
melittin; membrane-deformation; giant unilamellar liposome; real-time imaging; spectroscopic analysis
资金
- Ministry of Education, Culture, Sports, Science, and Technology of Japan [21015010, 24104004]
- Japan Society for the Promotion of Science [24651134]
- Grants-in-Aid for Scientific Research [24104004, 24651134, 21015010] Funding Source: KAKEN
Melittin induces various reactions in membranes and has been widely studied as a model for membrane-interacting peptide; however, the mechanism whereby melittin elicits its effects remains unclear. Here, we observed melittin-induced changes in individual giant liposomes using direct real-time imaging by dark-field optical microscopy, and the mechanisms involved were correlated with results obtained using circular dichroism, cosedimentation, fluorescence quenching of tryptophan residues, and electron microscopy. Depending on the concentration of negatively charged phospholipids in the membrane and the molecular ratio between lipid and melittin, melittin induced the increasing membrane area, phased shrinkage, or solubilization of liposomes. In phased shrinkage, liposomes formed small particles on their surface and rapidly decreased in size. Under conditions in which the increasing membrane area, phased shrinkage, or solubilization were mainly observed, the secondary structure of melittin was primarily estimated as an alpha-helix, beta-like, or disordered structure, respectively. When the increasing membrane area or phased shrinkage occurred, almost all melittin was bound to the membranes and reached more hydrophobic regions of the membranes than when solubilization occurred. These results indicate that the various effects of melittin result from its ability to adopt various structures and membrane-binding states depending on the conditions.
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