Dynamic nuclear polarization NMR spectroscopy was used to investigate the effect of the antimicrobial peptide (AMP) maculatin 1.1 on E. coli cells. The enhanced ^(15)N NMR signals from nucleic acids, proteins and lipids identified a number of unanticipated physiological responses to peptide stress, revealing that membrane-active AMPs can have a multi-target impact on E. coli cells. DNP-enhanced ^(15)N-observed ^(31)P-dephased REDOR NMR allowed monitoring how Mac1 induced DNA condensation and...
[NMR paper] NMR structure and localization of the host defense antimicrobial peptide thanatin in zwitterionic dodecylphosphocholine micelle: Implications in antimicrobial activity.
NMR structure and localization of the host defense antimicrobial peptide thanatin in zwitterionic dodecylphosphocholine micelle: Implications in antimicrobial activity.
NMR structure and localization of the host defense antimicrobial peptide thanatin in zwitterionic dodecylphosphocholine micelle: Implications in antimicrobial activity.
Biochim Biophys Acta Biomembr. 2020 Aug 08;:183432
Authors: Sinha S, Ng WJ, Bhattacharjya S
Abstract
Antimicrobial peptides (AMPs) are potentially vital as the next generation of antibiotics...
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[NMR paper] NMR model structure of the antimicrobial peptide maximin 3.
NMR model structure of the antimicrobial peptide maximin 3.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR model structure of the antimicrobial peptide maximin 3.
Eur Biophys J. 2019 Mar;48(2):203-212
Authors: Benetti S, Timmons PB, Hewage CM
Abstract
Maximin 3 is a 27-residue-long cationic antimicrobial peptide found in the skin secretion and brain of the Chinese red-belly toad Bombina maxima. The peptide is of biological...
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[NMR paper] High-resolution NMR structure of the antimicrobial peptide protegrin-2 in the presence of DPC micelles.
High-resolution NMR structure of the antimicrobial peptide protegrin-2 in the presence of DPC micelles.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles High-resolution NMR structure of the antimicrobial peptide protegrin-2 in the presence of DPC micelles.
J Biomol NMR. 2015 Apr;61(3-4):227-34
Authors: Usachev KS, Efimov SV, Kolosova OA, Filippov AV, Klochkov VV
Abstract
PG-1 adopts a dimeric structure in dodecylphosphocholine...
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High-resolution NMR structure of the antimicrobial peptide protegrin-2 in the presence of DPC micelles
High-resolution NMR structure of the antimicrobial peptide protegrin-2 in the presence of DPC micelles
Abstract
PG-1 adopts a dimeric structure in dodecylphosphocholine (DPC) micelles, and a channel is formed by the association of several dimers but the molecular mechanisms of the membrane damage by non-α-helical peptides are still unknown. The formation of the PG-1 dimer is important for pore formation in the lipid bilayer, since the dimer can be regarded as the primary unit for assembly into the ordered aggregates. It was supposed that only 12...
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Oligomeric Structure of a Cathelicidin Antimicrobial Peptide in Dodecylphosphocholine
Oligomeric Structure of a Cathelicidin Antimicrobial Peptide in Dodecylphosphocholine Micelle Determined by NMR Spectroscopy.
Related Articles Oligomeric Structure of a Cathelicidin Antimicrobial Peptide in Dodecylphosphocholine Micelle Determined by NMR Spectroscopy.
Biochim Biophys Acta. 2010 Oct 6;
Authors: Saravanan R, Bhattacharjya S
The broad spectrum of antibacterial activities of host defense cationic antimicrobial peptides (AMPs) arises from their ability to perturb membrane integrity of the microbes. The mechanisms are often thought to...
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10-12-2010 02:52 PM
19F NMR analysis of the antimicrobial peptide PGLa bound to native cell membranes fro
19F NMR analysis of the antimicrobial peptide PGLa bound to native cell membranes from bacterial protoplasts and human erythrocytes.
Related Articles 19F NMR analysis of the antimicrobial peptide PGLa bound to native cell membranes from bacterial protoplasts and human erythrocytes.
J Am Chem Soc. 2010 Jul 7;132(26):8822-4
Authors: Ieronimo M, Afonin S, Koch K, Berditsch M, Wadhwani P, Ulrich AS
(19)F NMR is a unique tool to examine the structure of fluorine-labeled peptides in their native cellular environment, due to an exquisite sensitivity...
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[NMR paper] Synthesis and structure determination by NMR of a putative vacuolar targeting peptide
Synthesis and structure determination by NMR of a putative vacuolar targeting peptide and model of a proteinase inhibitor from Nicotiana alata.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Synthesis and structure determination by NMR of a putative vacuolar targeting peptide and model of a proteinase inhibitor from Nicotiana alata.
Biochemistry. 1996 Jan 16;35(2):369-78
Authors: Nielsen KJ, Hill JM, Anderson MA, Craik DJ
NA-proPI is a 40.3-kDa multidomain precursor protein found in the...
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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...
In-cell DNP NMR reveals multiple targeting effect of antimicrobial peptide
Linear Mode
