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dc.contributor.author Whiles-Lillig, Jennifer en
dc.contributor.author Brasseur, Robert en
dc.contributor.author Glover, Kerney J. en
dc.contributor.author Melacini, Giuseppe en
dc.contributor.author Komives, Elizabeth A. en
dc.contributor.author Vold, Regitze R. en
dc.date.accessioned 2014-08-12T20:13:23Z en
dc.date.available 2014-08-12T20:13:23Z en
dc.date.issued 2001 en
dc.identifier.citation Whiles-Lillig, J.A., Brasseur, R., Glover, K.J., Melacini, G., Komives, E.A., Vold, R.R. 2001. "Orientation and Effects of Mastoparan X on Phospholipid Bicelles" Biophysical Journal. Vol 80 (2001): 280-293 en
dc.identifier.issn 0006-3495 en
dc.identifier.uri http://hdl.handle.net/10211.3/124828 en
dc.description Published by Cell Press on behalf of The Biophysical Society. Copyright of The Biophysical Society. The definitive version of this article is available at: http://www.sciencedirect.com/science/article/pii/S0006349501760134 en
dc.description.abstract Mastoparan X (MPX: INWKGIAAMAKKLL-NH2) belongs to a family of ionophoric peptides found in wasp venom. Upon binding to the membrane, MPX increases the cell’s permeability to cations leading to a disruption in the electrolyte balance and cell lysis. This process is thought to occur either through a membrane-thinning mechanism, where the peptide resides on the membrane surface thereby disrupting lipid packing, or through formation of an oligomeric pore. To address this issue, we have used both high-resolution and solid-state 2H NMR techniques to study the structure and orientation of MPX when associated with bicelles. NOESY and chemical shift analysis showed that in bicelles, MPX formed a well-structured amphipathic -helix. In zwitterionic bicelles, the helical axis was found to rest generally perpendicular to the membrane normal, which could be consistent with the “carpet” mechanism for lytic activity. In anionic bicelles, on the other hand, the helical axis was generally parallel to the membrane normal, which is more consistent with the pore model for lytic activity. In addition, MPX caused significant disruption in lipid packing of the negatively charged phospholipids. Taken together, these results show that MPX associates differently with zwitterionic membranes, where it rests parallel to the surface, compared with negatively charged membranes, where it penetrates longitudinally. en
dc.description.sponsorship This work was supported by National Institutes of Health (5 R01 GM54034) and National Science Foundation (award 9632618) grants to R.R.V. J.A.W. was supported by a La Jolla Interfaces in Science predoctoral fellowship from the Burroughs Wellcome Fund and an National Institutes of Health molecular biophysics training grant (T32 GM08326). en
dc.language.iso en_US en
dc.publisher Biophysical Journal en
dc.relation.uri http://www.sciencedirect.com/science/article/pii/S0006349501760134 en
dc.rights Copyright of The Biophysical Society en
dc.subject phospholipid bicelles en
dc.subject membranes en
dc.subject lipid packing en
dc.subject cell permeability en
dc.title Orientation and Effects of Mastoparan X on Phospholipid Bicelles en
dc.type Article en
dc.relation.journal Biophysical Journal en
dc.contributor.sonomaauthor Whiles-Lillig, Jennifer en

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