[NMR paper] Dimerization of the beta-Hairpin Membrane-Active Cationic Antimicrobial Peptide Capitellacin from Marine Polychaeta: An NMR Structural and Thermodynamic Study
Dimerization of the beta-Hairpin Membrane-Active Cationic Antimicrobial Peptide Capitellacin from Marine Polychaeta: An NMR Structural and Thermodynamic Study
Capitellacin is the ?-hairpin membrane-active cationic antimicrobial peptide from the marine polychaeta Capitella teleta. Capitellacin exhibits antibacterial activity, including against drug-resistant strains. To gain insight into the mechanism of capitellacin action, we investigated the structure of the peptide in the membrane-mimicking environment of dodecylphosphocholine (DPC) micelles using high-resolution NMR spectroscopy. In DPC solution, two structural forms of capitellacin were observed:...
[NMR paper] IN SITU SOLID-STATE NMR STUDY OF ANTIMICROBIAL PEPTIDE INTERACTIONs WITH ERYTHROCYTE MEMBRANES
IN SITU SOLID-STATE NMR STUDY OF ANTIMICROBIAL PEPTIDE INTERACTIONs WITH ERYTHROCYTE MEMBRANES
Antimicrobial peptides stand as promising therapeutics to mitigate the global rise of antibiotic resistance. They generally act by perturbing the bacterial cell membrane, and are thus less likely to induce resistance. Since they are membrane-active molecules, it is critical to verify and understand their potential action towards eukaryotic cells to help design effective and safe drugs. In this work, we studied the interaction of two antimicrobial peptides, aurein 1.2 and caerin 1.1, with red...
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[NMR paper] Oligomerization of the antimicrobial peptide Protegrin-5 in a membrane-mimicking environment. Structural studies by high-resolution NMR spectroscopy.
Oligomerization of the antimicrobial peptide Protegrin-5 in a membrane-mimicking environment. Structural studies by high-resolution NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Oligomerization of the antimicrobial peptide Protegrin-5 in a membrane-mimicking environment. Structural studies by high-resolution NMR spectroscopy.
Eur Biophys J. 2017 Apr;46(3):293-300
Authors: Usachev KS, Kolosova OA, Klochkova EA, Yulmetov AR,...
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03-21-2017 11:26 PM
[NMR paper] Structure and dynamics of a fusion peptide helical hairpin on the membrane surface: comparison of molecular simulations and NMR.
Structure and dynamics of a fusion peptide helical hairpin on the membrane surface: comparison of molecular simulations and NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Structure and dynamics of a fusion peptide helical hairpin on the membrane surface: comparison of molecular simulations and NMR.
J Phys Chem B. 2014 May 1;118(17):4461-70
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05-13-2015 12:28 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
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
[NMR paper] Motional dynamics of residues in a beta-hairpin peptide measured by 13C-NMR relaxatio
Motional dynamics of residues in a beta-hairpin peptide measured by 13C-NMR relaxation.
Related Articles Motional dynamics of residues in a beta-hairpin peptide measured by 13C-NMR relaxation.
Protein Sci. 1998 Mar;7(3):720-9
Authors: Ramirez-Alvarado M, Daragan VA, Serrano L, Mayo KH
Structurally characterizing partially folded peptides is problematic given the nature of their transient conformational states. 13C-NMR relaxation data can provide information on the geometry of bond rotations, motional restrictions, and correlated bond rotations...
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11-17-2010 11:06 PM
[NMR paper] An NMR study on the beta-hairpin region of barnase.
An NMR study on the beta-hairpin region of barnase.
Related Articles An NMR study on the beta-hairpin region of barnase.
Fold Des. 1996;1(3):231-41
Authors: Neira JL, Fersht AR
BACKGROUND: The beta-hairpin of barnase (residues Ser92-Leu95) has been proposed in theoretical and protein engineering studies to be an initiation site for folding . There is evidence for residual structure in this region from NMR studies of the denatured protein under different denaturing conditions . A more detailed analysis is possible by NMR studies of isolated...
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08-22-2010 02:27 PM
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...
Dimerization of the beta-Hairpin Membrane-Active Cationic Antimicrobial Peptide Capitellacin from Marine Polychaeta: An NMR Structural and Thermodynamic Study
Linear Mode
