Related ArticlesRecent progress on the application of (2)H solid-state NMR to probe the interaction of antimicrobial peptides with intact bacteria.
Biochim Biophys Acta. 2017 Aug 24;:
Authors: Booth V, Warschawski DE, Santisteban NP, Laadhari M, Marcotte I
Abstract
Discoveries relating to innate immunity and antimicrobial peptides (AMPs) granted Bruce Beutler and Jules Hoffmann a Nobel prize in medicine in 2011, and opened up new avenues for the development of therapies against infections, and even cancers. The mechanisms by which AMPs interact with, and ultimately disrupt, bacterial cell membranes is still, to a large extent, incompletely understood. Up until recently, this mechanism was studied using model lipid membranes that failed to reproduce the complexity of molecular interactions present in real cells comprising lipids but also membrane proteins, a cell wall containing peptidoglycan or lipopolysaccharides, and other molecules. In this review, we focus on recent attempts to study, at the molecular level, the interaction between cationic AMPs and intact bacteria, by (2)H solid-state NMR. Specifically-labeled lipids allow us to focus on the interaction of AMPs with the heart of the bacterial membrane, and measure the lipid order and its variation upon interaction with various peptides. We will review the important parameters to consider in such a study, and summarize the results obtained in the past 5years on various peptides, in particular aurein 1.2, caerin 1.1, MSI-78 and CA(1-8)M(1-10).
PMID: 28844739 [PubMed - as supplied by publisher]
[NMR paper] The application of DOSY NMR and molecular dynamics simulations to explore the mechanism(s) of micelle binding of antimicrobial peptides containing unnatural amino acids.
The application of DOSY NMR and molecular dynamics simulations to explore the mechanism(s) of micelle binding of antimicrobial peptides containing unnatural amino acids.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-7315-19-Wiley_FullText_120x30_orange.png Related Articles The application of DOSY NMR and molecular dynamics simulations to explore the mechanism(s) of micelle binding of antimicrobial peptides containing unnatural amino acids.
Biopolymers. 2013 Aug;99(8):548-61
Authors: Clark TD,...
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[NMR paper] REDOR solid-state NMR as a probe of the membrane locations of membrane-associated peptides and proteins.
REDOR solid-state NMR as a probe of the membrane locations of membrane-associated peptides and proteins.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif REDOR solid-state NMR as a probe of the membrane locations of membrane-associated peptides and proteins.
J Magn Reson. 2015 Apr;253:154-65
Authors: Jia L, Liang S, Sackett K, Xie L, Ghosh U, Weliky DP
Abstract
Rotational-echo double-resonance (REDOR) solid-state NMR is applied to probe the membrane...
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REDOR solid-state NMR as a probe of the membrane locations of membrane-associated peptides and proteins
REDOR solid-state NMR as a probe of the membrane locations of membrane-associated peptides and proteins
Publication date: April 2015
Source:Journal of Magnetic Resonance, Volume 253</br>
Author(s): Lihui Jia , Shuang Liang , Kelly Sackett , Li Xie , Ujjayini Ghosh , David P. Weliky</br>
Rotational-echo double-resonance (REDOR) solid-state NMR is applied to probe the membrane locations of specific residues of membrane proteins. Couplings are measured between protein 13CO nuclei and membrane lipid or cholesterol 2H and 31P nuclei. Specific 13CO labeling is used...
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03-20-2015 01:48 AM
[NMR paper] A 2H solid-state NMR study of lipid clustering by cationic antimicrobial and cell-penetrating peptides in model bacterial membranes.
A 2H solid-state NMR study of lipid clustering by cationic antimicrobial and cell-penetrating peptides in model bacterial membranes.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif Related Articles A 2H solid-state NMR study of lipid clustering by cationic antimicrobial and cell-penetrating peptides in model bacterial membranes.
Biophys J. 2013 Nov 19;105(10):2333-42
Authors: Kwon B, Waring AJ, Hong M
Abstract
Domain formation in bacteria-mimetic membranes...
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07-12-2014 04:28 AM
[NMR paper] Investigating the interaction between peptides of the amphipathic helix of Hcf106 and the phospholipid bilayer by solid-state NMR spectroscopy.
Investigating the interaction between peptides of the amphipathic helix of Hcf106 and the phospholipid bilayer by solid-state NMR spectroscopy.
Related Articles Investigating the interaction between peptides of the amphipathic helix of Hcf106 and the phospholipid bilayer by solid-state NMR spectroscopy.
Biochim Biophys Acta. 2013 Oct 18;
Authors: Zhang L, Liu L, Maltsev S, Lorigan GA, Dabney-Smith C
Abstract
The chloroplast twin arginine translocation (cpTat) system transports highly folded precursor proteins into the thylakoid lumen using...
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[NMR paper] Determining the mode of action involved in the antimicrobial activity of synthetic peptides: a solid-state NMR and FTIR study.
Determining the mode of action involved in the antimicrobial activity of synthetic peptides: a solid-state NMR and FTIR study.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif Related Articles Determining the mode of action involved in the antimicrobial activity of synthetic peptides: a solid-state NMR and FTIR study.
Biophys J. 2012 Oct 3;103(7):1470-9
Authors: Lorin A, Noël M, Provencher MÈ, Turcotte V, Cardinal S, Lagüe P, Voyer N, Auger M
Abstract
We have previously...
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03-01-2013 09:57 PM
Solution and Solid-State NMR Structural Studies of Antimicrobial Peptides LPcin-I and LPcin-II.
Solution and Solid-State NMR Structural Studies of Antimicrobial Peptides LPcin-I and LPcin-II.
Solution and Solid-State NMR Structural Studies of Antimicrobial Peptides LPcin-I and LPcin-II.
Biophys J. 2011 Sep 7;101(5):1193-201
Authors: Park TJ, Kim JS, Ahn HC, Kim Y
Abstract
Lactophoricin (LPcin-I) is an antimicrobial, amphiphatic, cationic peptide with 23-amino acid residues isolated from bovine milk. Its analogous peptide, LPcin-II, lacks six N-terminal amino acids compared to LPcin-I. Interestingly, LPcin-II does not display any...
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Long-Term-Stable Ether-Lipid vs Conventional Ester-Lipid Bicelles in Oriented Solid-State NMR: Altered Structural Information in Studies of Antimicrobial Peptides.
Long-Term-Stable Ether-Lipid vs Conventional Ester-Lipid Bicelles in Oriented Solid-State NMR: Altered Structural Information in Studies of Antimicrobial Peptides.
Long-Term-Stable Ether-Lipid vs Conventional Ester-Lipid Bicelles in Oriented Solid-State NMR: Altered Structural Information in Studies of Antimicrobial Peptides.
J Phys Chem B. 2011 Feb 10;
Authors: Bertelsen K, Vad B, Nielsen EH, Hansen SK, Skrydstrup T, Otzen DE, Vosegaard T, Nielsen NC
Recently, ether lipids have been introduced as long-term stable alternatives to the more natural,...
Recent progress on the application of (2)H solid-state NMR to probe the interaction of antimicrobial peptides with intact bacteria.
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