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On the Role of NMR Spectroscopy for Characterization of Antimicrobial Peptides

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Membrane Proteins

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1063))

Abstract

Antimicrobial peptides (AMPs) provide a primordial source of immunity, conferring upon eukaryotic cells resistance against bacteria, protozoa, and viruses. Despite a few examples of anionic peptides, AMPs are usually relatively short positively charged polypeptides, consisting of a dozen to about a hundred amino acids, and exhibiting amphipathic character. Despite significant differences in their primary and secondary structures, all AMPs discovered to date share the ability to interact with cellular membranes, thereby affecting bilayer stability, disrupting membrane organization, and/or forming well-defined pores. AMPs selectively target infectious agents without being susceptible to any of the common pathways by which these acquire resistance, thereby making AMPs prime candidates to provide therapeutic alternatives to conventional drugs. However, the mechanisms of AMP actions are still a matter of intense debate. The structure–function paradigm suggests that a better understanding of how AMPs elicit their biological functions could result from atomic resolution studies of peptide–lipid interactions. In contrast, more strict thermodynamic views preclude any roles for three-dimensional structures. Indeed, the design of selective AMPs based solely on structural parameters has been challenging. In this chapter, we will focus on selected AMPs for which studies on the corresponding AMP–lipid interactions have helped reach an understanding of how AMP effects are mediated. We will emphasize the roles of both liquid- and solid-state NMR spectroscopy for elucidating the mechanisms of action of AMPs.

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Acknowledgement

This work is partially supported by the National Institute of Health (GM 64742 to G.V.).

Author information

Authors and Affiliations

  1. Department of Chemistry, University of Minnesota, Minneapolis, MN, USA

    Fernando Porcelli, George Barany & Gianluigi Veglia

  2. Department of Biochemistry, Molecular Biology, & Biophysics, University of Minnesota, Minneapolis, MN, USA

    Fernando Porcelli & Gianluigi Veglia

  3. Department of Chemistry, University of Michigan, Ann Arbor, MI, USA

    Ayyalusamy Ramamoorthy

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  1. Fernando Porcelli
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  2. Ayyalusamy Ramamoorthy
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  3. George Barany
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  4. Gianluigi Veglia
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Editors and Affiliations

  1. Dept. of Chemistry and Biochemistry, Arizona State University, Tempe, Arizona, USA

    Giovanna Ghirlanda

  2. Department of Biochemistry, University of Wisconsin, Madison, Madison, Wisconsin, USA

    Alessandro Senes

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Porcelli, F., Ramamoorthy, A., Barany, G., Veglia, G. (2013). On the Role of NMR Spectroscopy for Characterization of Antimicrobial Peptides. In: Ghirlanda, G., Senes, A. (eds) Membrane Proteins. Methods in Molecular Biology, vol 1063. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-583-5_9

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  • DOI: https://doi.org/10.1007/978-1-62703-583-5_9

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  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-1-62703-582-8

  • Online ISBN: 978-1-62703-583-5

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