Antimicrobial peptides (AMPs) have been a topic of substantial research as the next-generation antibiotics. They have been extensively studied for the selectivity and action against microbial membrane lipids in imparting their targeted functioning. To determine the effectivity of the peptides against the Gram-negative pathogens, it is imperative to elucidate their role in interacting with the lipopolysaccharide moieties. Lipopolysaccharide is a major component of the outer membrane of the...
[NMR paper] Structures of Pathological and Functional Amyloids and Prions, a Solid-State NMR Perspective
Structures of Pathological and Functional Amyloids and Prions, a Solid-State NMR Perspective
Infectious proteins or prions are a remarkable class of pathogens, where pathogenicity and infectious state correspond to conformational transition of a protein fold. The conformational change translates into the formation by the protein of insoluble amyloid aggregates, associated in humans with various neurodegenerative disorders and systemic protein-deposition diseases. The prion principle, however, is not limited to pathogenicity. While pathological amyloids (and prions) emerge from protein...
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[NMR paper] Preparation of Membrane Models of Gram-Negative Bacteria and Their Interaction with Antimicrobial Peptides Studied by CD and NMR.
Preparation of Membrane Models of Gram-Negative Bacteria and Their Interaction with Antimicrobial Peptides Studied by CD and NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Preparation of Membrane Models of Gram-Negative Bacteria and Their Interaction with Antimicrobial Peptides Studied by CD and NMR.
Methods Mol Biol. 2017;1548:231-245
Authors: Hicks R
Abstract
The antibiotic activity of antimicrobial peptides is generally...
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[NMR paper] Interaction of the antimicrobial peptides caerin 1.1 and aurein 1.2 with intact bacteria by (2)H solid-state NMR.
Interaction of the antimicrobial peptides caerin 1.1 and aurein 1.2 with intact bacteria by (2)H solid-state NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Interaction 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...
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[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...
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[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,...
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[NMR paper] NMR Structures and Interactions of Antimicrobial Peptides with Lipopolysaccharide: Connecting Structures to Functions.
NMR Structures and Interactions of Antimicrobial Peptides with Lipopolysaccharide: Connecting Structures to Functions.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.eurekaselect.com-sites-all-themes-eurekaselect-images-ben_pubmed_flag1.gif Related Articles NMR Structures and Interactions of Antimicrobial Peptides with Lipopolysaccharide: Connecting Structures to Functions.
Curr Top Med Chem. 2016;16(1):4-15
Authors: Bhattacharjya S
Abstract
Antimicrobial peptides (AMPs) establish the first line...
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06-23-2016 10:34 AM
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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Probing membrane topology of the antimicrobial peptide distinctin by solid-state NMR
Probing membrane topology of the antimicrobial peptide distinctin by solid-state NMR spectroscopy in zwitterionic and charged lipid bilayers.
Related Articles Probing 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...
Probing the Functional Interaction Interface of Lipopolysaccharide and Antimicrobial Peptides: A Solution-State NMR Perspective
Linear Mode
