CHAPTER 14: NMR Investigations of the Structure and Dynamics of Antimicrobial Peptides: The Peptaibol Alamethicin
Published:24 Feb 2014
T. Vosegaard and N. C. Nielsen, in Advances in Biological Solid-State NMR: Proteins and Membrane-Active Peptides, ed. F. Separovic and A. Naito, The Royal Society of Chemistry, 2014, pp. 267-286.
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Antimicrobial peptides are part of the biological defense system and potentially interesting targets for treatment of infections. As such, it is of great interest to understand their function and explore ways to make them better drug targets. In this chapter, we review some recent efforts in understanding the function of the peptaibol alamethicin using liquid- and solid-state NMR spectroscopy in combination with MD simulations. Our studies reveal the complexity and highly dynamic features of antimicrobial peptides and demonstrate that, by combining different experimental techniques, it is possible to establish putative models for the mode of action of the antimicrobial peptide. In addition, we show that it is possible to improve peptide function through scaffolding onto cyclodextrin rings, thereby altering the peptide interactions and the channel formation propensity.