Multiple Membrane Interactions and Versatile Vesicle Deformations Elicited by Melittin
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 imagin...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2013-04-01
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| Series: | Toxins |
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| Online Access: | http://www.mdpi.com/2072-6651/5/4/637 |
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| author | Kingo Takiguchi Michio Homma Yasunori Yokoyama Yohko Tanaka-Takiguchi Tomoyoshi Takahashi Fumimasa Nomura |
| author_facet | Kingo Takiguchi Michio Homma Yasunori Yokoyama Yohko Tanaka-Takiguchi Tomoyoshi Takahashi Fumimasa Nomura |
| author_sort | Kingo Takiguchi |
| collection | DOAJ |
| description | 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 α-helix, β-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. |
| first_indexed | 2024-04-11T21:45:20Z |
| format | Article |
| id | doaj.art-dd358646946a4f839032c4b624c99c0b |
| institution | Directory Open Access Journal |
| issn | 2072-6651 |
| language | English |
| last_indexed | 2024-04-11T21:45:20Z |
| publishDate | 2013-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Toxins |
| spelling | doaj.art-dd358646946a4f839032c4b624c99c0b2022-12-22T04:01:27ZengMDPI AGToxins2072-66512013-04-015463766410.3390/toxins5040637Multiple Membrane Interactions and Versatile Vesicle Deformations Elicited by MelittinKingo TakiguchiMichio HommaYasunori YokoyamaYohko Tanaka-TakiguchiTomoyoshi TakahashiFumimasa NomuraMelittin 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 α-helix, β-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.http://www.mdpi.com/2072-6651/5/4/637melittinmembrane-deformationgiant unilamellar liposomereal-time imagingspectroscopic analysis |
| spellingShingle | Kingo Takiguchi Michio Homma Yasunori Yokoyama Yohko Tanaka-Takiguchi Tomoyoshi Takahashi Fumimasa Nomura Multiple Membrane Interactions and Versatile Vesicle Deformations Elicited by Melittin Toxins melittin membrane-deformation giant unilamellar liposome real-time imaging spectroscopic analysis |
| title | Multiple Membrane Interactions and Versatile Vesicle Deformations Elicited by Melittin |
| title_full | Multiple Membrane Interactions and Versatile Vesicle Deformations Elicited by Melittin |
| title_fullStr | Multiple Membrane Interactions and Versatile Vesicle Deformations Elicited by Melittin |
| title_full_unstemmed | Multiple Membrane Interactions and Versatile Vesicle Deformations Elicited by Melittin |
| title_short | Multiple Membrane Interactions and Versatile Vesicle Deformations Elicited by Melittin |
| title_sort | multiple membrane interactions and versatile vesicle deformations elicited by melittin |
| topic | melittin membrane-deformation giant unilamellar liposome real-time imaging spectroscopic analysis |
| url | http://www.mdpi.com/2072-6651/5/4/637 |
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