Beyond NMR spectra of antimicrobial peptides: dynamical images at atomic resolution and functional insights.
TLDR
Solid-state NMR studies of antimicrobial peptides that have reported high-resolution structure, dynamics, orientation, and oligomeric states of antimacterial peptides in a membrane environment are discussed, and important questions about the mechanism of action at atomic-level resolution are addressed.About:
This article is published in Solid State Nuclear Magnetic Resonance.The article was published on 2009-07-01 and is currently open access. It has received 141 citations till now. The article focuses on the topics: Antimicrobial peptides & Nuclear magnetic resonance spectroscopy.read more
Citations
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The magic of bicelles lights up membrane protein structure.
TL;DR: Recent advances in the field of protein structural biology that have been made possible by exploiting the unique properties of lipid bicelles, in both solution and solid-state NMR spectroscopy, will be discussed.
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Biomimetic antimicrobial polymers: recent advances in molecular design
TL;DR: The key macromolecular design principles that have been gleaned from more than a decade of structure–activity relationship (SAR) studies, as well as some key mechanistic investigations, across this multidisciplinary field are focused on.
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Chemical Shift Tensor – the Heart of NMR: Insights into Biological Aspects of Proteins
TL;DR: The resonance NMR frequency, νi, of a given nucleus in a molecule is thus related to its gyromagnetic ratio, γi, as given by in normal NMR experiments B0 is a uniform field along the z-axis; therefore, σi= σizz.
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Solid‐State NMR Spectroscopy on Complex Biomolecules
TL;DR: This Review discusses current approaches and methodological challenges, and highlights recent progress in using ssNMR spectroscopy at the interface of structural and cellular biology.
References
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Antimicrobial peptides of multicellular organisms
TL;DR: As the need for new antibiotics becomes more pressing, could the design of anti-infective drugs based on the design principles these molecules teach us?
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Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides.
TL;DR: This review, which is focused on the different stages of membrane permeation induced by representatives of amphipathic alpha-helical antimicrobial and cell non-selective lytic peptides distinguishes between the 'carpet' mechanism, which holds for antimicrobial peptides versus the 'barrel-stave' mechanisms, which hold for cellnon- selective lytics peptides.
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Multidimensional solid-state NMR and polymers
TL;DR: In this paper, the authors present a review of the structure and dynamics of polymers using multidimensional NMR and derive a determination of order in polymers by multi-dimensional NMR.
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Diversity of antimicrobial peptides and their mechanisms of action.
Richard M. Epand,Hans J. Vogel +1 more
TL;DR: It is not likely that this diverse group of peptides has a single mechanism of action, but interaction of the peptides with membranes is an important requirement for most, if not all, antimicrobial peptides.