Related ArticlesInteraction of the antimicrobial peptides caerin 1.1 and aurein 1.2 with intact bacteria by (2)H solid-state NMR.
Biochim Biophys Acta. 2016 12;1858(12):2959-2964
Authors: Laadhari M, Arnold AA, Gravel AE, Separovic F, Marcotte I
Abstract
Nuclear magnetic resonance (NMR) is commonly used to probe the effect of antimicrobial agents on bacterial membranes using model membrane systems. Ideally, considering the complexity of membranes, the interaction of molecules with membranes should be studied in vivo. The interactions of two antimicrobial peptides (AMPs) with intact Escherichia coli and Bacillus subtilis were investigated using deuterium solid-state NMR. Specifically, we studied caerin 1.1 and aurein 1.2 isolated from the skin of Australian tree frogs. The minimal inhibitory concentration value for E. coli and B. subtilis was about 100?g/mL and 30?g/mL, respectively, for both peptides. A protocol to deuterate the membrane phospholipids of non-mutated B. subtilis was established using deuterated palmitic acid. (2)H NMR spectra combined with spectral moment analysis support the interaction of the two AMPs with the hydrophobic core of the bacterial membranes. The presence of peptides decreased the order of the lipid acyl chains for both E. coli and B. subtilis, but at higher peptide concentrations for the Gram(+) bacteria. This may be explained by the presence of other cell wall components, such as the negatively-charged teichoic and lipoteichoic acids in the peptidoglycan, which would interact with the AMPs and decrease their actual concentration on the membrane surface. The mechanism of action of the AMPs thus depends on their local concentration as well as the membrane environment. The differences between the AMPs interaction with E. coli and B. subtilis reveal the importance of studying intact bacteria.
[NMR paper] Recent progress on the application of (2)H solid-state NMR to probe the interaction of antimicrobial peptides with intact bacteria.
Recent progress on the application of (2)H solid-state NMR to probe the interaction of antimicrobial peptides with intact bacteria.
Related Articles Recent 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...
nmrlearner
Journal club
0
08-29-2017 05:35 PM
[NMR paper] Determination of Structure and Micellar Interactions of Small Antimicrobial Peptides by Solution-State NMR.
Determination of Structure and Micellar Interactions of Small Antimicrobial Peptides by Solution-State NMR.
Related Articles Determination of Structure and Micellar Interactions of Small Antimicrobial Peptides by Solution-State NMR.
Methods Mol Biol. 2017;1548:73-88
Authors: Wimmer R, Uggerhøj LE
Abstract
NMR spectroscopy is a well-established technique to determine the structure of peptides and small proteins in solution, also when bound to detergent micelles or phospholipid bicelles. The structure of the peptide alone is,...
nmrlearner
Journal club
0
12-26-2016 12:50 PM
[NMR paper] Structural basis of a temporin 1b analogue antimicrobial activity against Gram negative bacteria determined by CD and NMR techniques in cellular environment.
Structural basis of a temporin 1b analogue antimicrobial activity against Gram negative bacteria determined by CD and NMR techniques in cellular environment.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Structural basis of a temporin 1b analogue antimicrobial activity against Gram negative bacteria determined by CD and NMR techniques in cellular environment.
ACS Chem Biol. 2015 Apr 17;10(4):965-9
Authors: Malgieri G, Avitabile C, Palmieri M, D'Andrea LD, Isernia C,...
nmrlearner
Journal club
0
05-04-2016 01:47 PM
[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...
nmrlearner
Journal club
0
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...
nmrlearner
Journal club
0
10-23-2013 05:10 PM
[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...
nmrlearner
Journal club
0
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...
nmrlearner
Journal club
0
09-06-2011 06:02 PM
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,...
Interaction of the antimicrobial peptides caerin 1.1 and aurein 1.2 with intact bacteria by (2)H solid-state NMR.
Linear Mode
