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Please use this identifier to cite or link to this item: http://hdl.handle.net/1959.3/157980
- Structural dynamics of a lytic peptide interacting with a supported lipid bilayer
- Rapson, Andrew C.; Hossain, Mohammed Akhter; Wade, John D.; Nice, Edouard C.; Smith, Trevor A.; Clayton, Andrew H. A.; Gee, Michelle L.
- The interaction of a melittin mutant with a 1,2-dipalmitoyl-sn-glycero-3-phosphatidylcholine (DPPC)-supported lipid bilayer was studied with the use of time-resolved evanescent wave-induced fluorescence spectroscopy (TREWIFS) and evanescent wave-induced time-resolved fluorescence anisotropy measurements (EW-TRAMs). The mutant peptide was labeled at position K14 with AlexaFluor 430 and retained the lytic activity characteristic of native melittin. The fluorescence decay kinetics of the conjugate was found to be biexponential with a short-lived component, tau(1), due to photoinduced electron transfer between AlexaFluor 430 and proximal side chains within or between the peptides. The longer-lived component, tau(2), was sensitive to the polarity of the microenvironment at or near the K14 position of the peptide. Upon interaction with a DPPC-supported bilayer, the proportional contribution of tau(1) increased, indicating a conformational change of the peptide. The values of tau(1) and tau(2) indicate that the AlexaFluor 430 probe experienced an environment with an equivalent polarity no less than that of methanol. EW-TRAMs data from the melittin mutant revealed hindered rotational motions of the AlexaFluor 430 probe both in the plane and perpendicular to the plane of the supported lipid bilayer. The data indicate a highly ordered and polar environment near the center of the melittin helix consistent with the formation of a toroidal pore.
- Publication type
- Journal article
- Research centre
- Swinburne University of Technology. Faculty of Engineering and Industrial Sciences. Centre for Micro-Photonics
- Biophysical Journal, Vol. 100, no. 5 (Mar 2011), pp. 1353-1361
- Publication year
- Cell Press
- Publisher URL
- Copyright © 2011.