Marine sponge cyclic peptide theonellamide A disrupts lipid bilayer integrity without forming distinct membrane pores
College
College of Science
Department/Unit
Chemistry
Document Type
Article
Source Title
Biochimica et Biophysica Acta - Biomembranes
Volume
1858
Issue
6
First Page
1373
Last Page
1379
Publication Date
6-1-2016
Abstract
Theonellamides (TNMs) are antifungal and cytotoxic bicyclic dodecapeptides derived from the marine sponge Theonella sp. These peptides specifically bind to 3β-hydroxysterols, resulting in 1,3-β-d-glucan overproduction and membrane damage in yeasts. The inclusion of cholesterol or ergosterol in phosphatidylcholine membranes significantly enhanced the membrane affinity of theonellamide A (TNM-A) because of its direct interaction with 3β-hydroxyl groups of sterols. To better understand TNM-induced membrane alterations, we investigated the effects of TNM-A on liposome morphology. 31P nuclear magnetic resonance (NMR) and dynamic light scattering (DLS) measurements revealed that the premixing of TNM-A with lipids induced smaller vesicle formation. When giant unilamellar vesicles were incubated with exogenously added TNM-A, confocal micrographs showed dynamic changes in membrane morphology, which were more frequently observed in cholesterol-containing than sterol-free liposomes. In conjunction with our previous data, these results suggest that the membrane action of TNM-A proceeds in two steps: 1) TNM-A binds to the membrane surface through direct interaction with sterols and 2) accumulated TNM-A modifies the local membrane curvature in a concentration-dependent manner, resulting in dramatic membrane morphological changes and membrane disruption. © 2016 Elsevier B.V. All rights reserved.
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Digitial Object Identifier (DOI)
10.1016/j.bbamem.2016.03.019
Recommended Citation
Espiritu, R. A., Cornelio, K., Kinoshita, M., Matsumori, N., Murata, M., Nishimura, S., Kakeya, H., Yoshida, M., & Matsunaga, S. (2016). Marine sponge cyclic peptide theonellamide A disrupts lipid bilayer integrity without forming distinct membrane pores. Biochimica et Biophysica Acta - Biomembranes, 1858 (6), 1373-1379. https://doi.org/10.1016/j.bbamem.2016.03.019
Disciplines
Chemistry
Keywords
Oligopeptides; Peptides; Sponges; Liposomes; Bilayer lipid membranes
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