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Probing Melittin Helix−Coil Equilibria in Solutions and Vesicles

Hartings, Matthew R. and Gray, Harry B. and Winkler, Jay R. (2008) Probing Melittin Helix−Coil Equilibria in Solutions and Vesicles. Journal of Physical Chemistry B, 112 (10). pp. 3202-3207. ISSN 1520-6106. doi:10.1021/jp709866g.

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Melittin is a toxic, amphipathic peptide that rearranges from a random coil in solution to a helical structure upon binding to cell membranes or lipid vesicles. We have found that mutation of the valine at position five of the peptide to a phenylalanine or 3-nitrotyrosine induces aggregation and helix formation at low concentrations (20−80 μM). Donor−acceptor distances obtained from analyses of fluorescence energy transfer kinetics experiments with the 3-nitrotyrosine mutant indicate that both coil and helix structures are present in 2 and 20 μM aqueous solutions. The helical peptide population increases upon addition of phospholipid vesicles or in high ionic strength solutions.

Item Type:Article
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Gray, Harry B.0000-0002-7937-7876
Winkler, Jay R.0000-0002-4453-9716
Additional Information:© 2008 American Chemical Society. Received 9 October 2007. Published online 21 February 2008. Published in print 1 March 2008. This work was supported by NIH (GM068461 to J.R.W., GM078792A to M.R.H.), Ellison Medical Foundation (Senior Scholar Award in Aging to H.B.G.), and the Arnold and Mabel Beckman Foundation.
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Ellison Medical FoundationUNSPECIFIED
Arnold and Mabel Beckman FoundationUNSPECIFIED
Issue or Number:10
Record Number:CaltechAUTHORS:20170717-151917379
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Official Citation:Probing Melittin Helix−Coil Equilibria in Solutions and Vesicles Matthew R. Hartings, Harry B. Gray, and Jay R. Winkler The Journal of Physical Chemistry B 2008 112 (10), 3202-3207 DOI: 10.1021/jp709866g
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:79136
Deposited By: Ruth Sustaita
Deposited On:17 Jul 2017 22:49
Last Modified:15 Nov 2021 17:45

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