Related ArticlesProbing membrane topology of the antimicrobial peptide distinctin by solid-state NMR spectroscopy in zwitterionic and charged lipid bilayers.
Biochim Biophys Acta. 2010 Aug 15;
Authors: Verardi R, Traaseth NJ, Shi L, Porcelli F, Monfregola L, De Luca S, Amodeo P, Veglia G, Scaloni A
Distinctin is a 47-residue antimicrobial peptide, which interacts with negatively charged membranes and is active against Gram-positive and Gram-negative bacteria. Its primary sequence comprises two linear chains of 22 (chain 1) and 25 (chain 2) residues, linked by a disulfide bridge between Cys19 of chain 1 and Cys23 of chain 2. Unlike other antimicrobial peptides, distinctin in the absence of the lipid membrane has a well-defined three-dimensional structure, which protects it from protease degradation. Here, we used static solid-state NMR spectroscopy to study the topology of distinctin in lipid bilayers. We found that In mechanically aligned lipid bilayers (charged or zwitterionic ) this heterodimeric peptide adopts an ordered conformation absorbed on the surface of the membrane, with the long helix (chain 2), approximately parallel to the lipid bilayer (~5 masculine from the membrane plane) and the short helix (chain 1) forming a ~24 masculine angle. Since at lipid-to-protein molar ratio of 50:1 the peptide does not disrupt the macroscopic alignment of either charged or zwitterionic lipid bilayers, it is possible that higher concentrations might be needed for the hypothesized pore formation, or alternatively, distinctin elicits its cell disruption action by other mechanisms.
PMID: 20719234 [PubMed - as supplied by publisher]
Membrane binding of an acyl-lactoferricin B antimicrobial peptide from solid-state NMR experiments and molecular dynamics simulations.
Membrane binding of an acyl-lactoferricin B antimicrobial peptide from solid-state NMR experiments and molecular dynamics simulations.
Membrane binding of an acyl-lactoferricin B antimicrobial peptide from solid-state NMR experiments and molecular dynamics simulations.
Biochim Biophys Acta. 2011 Aug;1808(8):2019-30
Authors: Romo TD, Bradney LA, Greathouse DV, Grossfield A
Abstract
One approach to the growing health problem of antibiotic resistant bacteria is the development of antimicrobial peptides (AMPs) as alternative treatments. The...
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08-19-2011 02:56 PM
A kinked antimicrobial peptide from Bombina maxima. I. Three-dimensional structure determined by NMR in membrane-mimicking environments.
A kinked antimicrobial peptide from Bombina maxima. I. Three-dimensional structure determined by NMR in membrane-mimicking environments.
A kinked antimicrobial peptide from Bombina maxima. I. Three-dimensional structure determined by NMR in membrane-mimicking environments.
Eur Biophys J. 2011 Apr;40(4):447-62
Authors: Toke O, Bánóczi Z, Király P, Heinzmann R, Bürck J, Ulrich AS, Hudecz F
Maximin-4 is a 27-residue cationic antimicrobial peptide exhibiting selectivity for bacterial cells. As part of the innate defense system in the Chinese red-belly...
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07-20-2011 10:00 AM
Structure and alignment of the membrane-associated antimicrobial peptide arenicin by oriented solid-state NMR spectroscopy.
Structure and alignment of the membrane-associated antimicrobial peptide arenicin by oriented solid-state NMR spectroscopy.
Structure and alignment of the membrane-associated antimicrobial peptide arenicin by oriented solid-state NMR spectroscopy.
Biochemistry. 2011 May 10;50(18):3784-95
Authors: Salnikov ES, Aisenbrey C, Balandin SV, Zhmak MN, Ovchinnikova TV, Bechinger B
The antimicrobial arenicin peptides are cationic amphipathic sequences that strongly interact with membranes. Through a cystine ring closure a cyclic ?-sheet structure is formed...
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07-13-2011 06:42 PM
Structure and Alignment of the Membrane-Associated Antimicrobial Peptide Arenicin by Oriented Solid-State NMR Spectroscopy
Structure and Alignment of the Membrane-Associated Antimicrobial Peptide Arenicin by Oriented Solid-State NMR Spectroscopy
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi1018732/aop/images/medium/bi-2010-018732_0008.gif
Biochemistry
DOI: 10.1021/bi1018732
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04-16-2011 02:04 AM
NMR structures of the histidine-rich peptide LAH4 in micellar environments: membrane insertion, pH-dependent mode of antimicrobial action, and DNA transfection.
NMR structures of the histidine-rich peptide LAH4 in micellar environments: membrane insertion, pH-dependent mode of antimicrobial action, and DNA transfection.
NMR structures of the histidine-rich peptide LAH4 in micellar environments: membrane insertion, pH-dependent mode of antimicrobial action, and DNA transfection.
Biophys J. 2010 Oct 20;99(8):2507-15
Authors: Georgescu J, Munhoz VH, Bechinger B
The LAH4 family of histidine-rich peptides exhibits potent antimicrobial and DNA transfection activities, both of which require interactions...
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02-02-2011 02:40 AM
[NMR paper] Membrane insertion of a lipidated ras peptide studied by FTIR, solid-state NMR, and n
Membrane insertion of a lipidated ras peptide studied by FTIR, solid-state NMR, and neutron diffraction spectroscopy.
Related Articles Membrane insertion of a lipidated ras peptide studied by FTIR, solid-state NMR, and neutron diffraction spectroscopy.
J Am Chem Soc. 2003 Apr 9;125(14):4070-9
Authors: Huster D, Vogel A, Katzka C, Scheidt HA, Binder H, Dante S, Gutberlet T, Zschörnig O, Waldmann H, Arnold K
Membrane binding of a doubly lipid modified heptapeptide from the C-terminus of the human N-ras protein was studied by Fourier transform...
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11-24-2010 09:01 PM
[NMR paper] Membrane protein topology probed by (1)H spin diffusion from lipids using solid-state
Membrane protein topology probed by (1)H spin diffusion from lipids using solid-state NMR spectroscopy.
Related Articles Membrane protein topology probed by (1)H spin diffusion from lipids using solid-state NMR spectroscopy.
J Am Chem Soc. 2002 Feb 6;124(5):874-83
Authors: Huster D, Yao X, Hong M
We describe a two-dimensional solid-state NMR technique to investigate membrane protein topology under magic-angle spinning conditions. The experiment detects the rate of (1)H spin diffusion from the mobile lipids to the rigid protein. While spin...
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11-24-2010 08:49 PM
[NMR paper] A solid-state NMR index of helical membrane protein structure and topology.
A solid-state NMR index of helical membrane protein structure and topology.
Related Articles A solid-state NMR index of helical membrane protein structure and topology.
J Magn Reson. 2000 May;144(1):150-5
Authors: Marassi FM, Opella SJ
The secondary structure and topology of membrane proteins can be described by inspection of two-dimensional (1)H-(15)N dipolar coupling/(15)N chemical shift polarization inversion spin exchange at the magic angle spectra obtained from uniformly (15)N-labeled samples in oriented bilayers. The characteristic...
Probing membrane topology of the antimicrobial peptide distinctin by solid-state NMR
Linear Mode
