[NMR paper] Oligomerization of the antimicrobial peptide Protegrin-5 in a membrane-mimicking environment. Structural studies by high-resolution NMR spectroscopy.
Related ArticlesOligomerization of the antimicrobial peptide Protegrin-5 in a membrane-mimicking environment. Structural studies by high-resolution NMR spectroscopy.
Abstract
Protegrin pore formation is believed to occur in a stepwise fashion that begins with a nonspecific peptide interaction with the negatively charged bacterial cell walls via hydrophobic and positively charged amphipathic surfaces. There are five known nature protegrins (PG1-PG5), and early studies of PG-1 (PDB ID:1PG1) shown that it could form antiparallel dimer in membrane mimicking environment which could be a first step for further oligomeric membrane pore formation. Later, we solved PG-2 (PDB ID:2MUH) and PG-3 (PDB ID:2MZ6) structures in the same environment and for PG-3 observed a strong d?? NOE effects between residues R18 and F12, V14, and V16. These "inconsistent" with monomer structure NOEs appears due to formation of an additional antiparallel ?-sheet between two monomers. It was also suggested that there is a possible association of protegrins dimers to form octameric or decameric ?-barrels in an oligomer state. In order to investigate a more detailed oligomerization process of protegrins, in the present article we report the monomer (PDB ID: 2NC7) and octamer pore structures of the protegrin-5 (PG-5) in the presence of DPC micelles studied by solution NMR spectroscopy. In contrast to PG-1, PG-2, and PG-3 studies, for PG-5 we observed not only dimer NOEs but also several additional NOEs between side chains, which allows us to calculate an octamer pore structure of PG-5 that was in good agreement with previous AFM and PMF data.
[NMR paper] Antimicrobial peptide protegrin-3 adopt an antiparallel dimer in the presence of DPC micelles: a high-resolution NMR study.
Antimicrobial peptide protegrin-3 adopt an antiparallel dimer in the presence of DPC micelles: a high-resolution NMR study.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Antimicrobial peptide protegrin-3 adopt an antiparallel dimer in the presence of DPC micelles: a high-resolution NMR study.
J Biomol NMR. 2015 May;62(1):71-9
Authors: Usachev KS, Efimov SV, Kolosova OA, Klochkova EA, Aganov AV, Klochkov VV
Abstract
A tendency...
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03-26-2016 12:14 PM
[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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02-03-2016 10:22 PM
Antimicrobial peptide protegrin-3 adopt an antiparallel dimer in the presence of DPC micelles: a high-resolution NMR study
Antimicrobial peptide protegrin-3 adopt an antiparallel dimer in the presence of DPC micelles: a high-resolution NMR study
Abstract
A tendency to dimerize in the presence of lipids was found for the protegrin. The dimer formation by the protegrin-1 (PG-1) is the first step for further oligomeric membrane pore formation. Generally there are two distinct model of PG-1 dimerization in either a parallel or antiparallel β-sheet. But despite the wealth of data available today, protegrin dimer structure and pore formation is still not completely understood....
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03-19-2015 07:38 AM
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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11-28-2014 11:37 AM
[NMR paper] NMR solution structure and condition-dependent oligomerization of the antimicrobial peptide human defensin 5.
NMR solution structure and condition-dependent oligomerization of the antimicrobial peptide human defensin 5.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles NMR solution structure and condition-dependent oligomerization of the antimicrobial peptide human defensin 5.
Biochemistry. 2012 Dec 4;51(48):9624-37
Authors: Wommack AJ, Robson SA, Wanniarachchi YA, Wan A, Turner CJ, Wagner G, Nolan EM
Abstract
Human defensin 5 (HD5) is a 32-residue host-defense peptide...
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03-30-2013 12:59 PM
NMR Solution Structure and Condition-Dependent Oligomerization of the Antimicrobial Peptide Human Defensin 5
NMR Solution Structure and Condition-Dependent Oligomerization of the Antimicrobial Peptide Human Defensin 5
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi301255u/aop/images/medium/bi-2012-01255u_0008.gif
Biochemistry
DOI: 10.1021/bi301255u
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11-20-2012 04:20 AM
NMR characterization of the C-terminal tail of full-length RAGE in a membrane mimicking environment
NMR characterization of the C-terminal tail of full-length RAGE in a membrane mimicking environment
Abstract Targeting the receptor for the advanced glycation endproducts (RAGE) signalling has a potential for the prevention and treatment of several pathologies. Extracellular activation of RAGE triggers the interactions of the RAGE cytoplasmic tail with intracellular protein partners. Here the cytoplasmic tail of RAGE has been investigated by NMR as part of the full-length protein, in the presence of a membrane-mimicking environment. The isolated cytoplasmic tail has also been studied...
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09-24-2012 01:02 AM
A kinked antimicrobial peptide from Bombina maxima. I. Three-dimensional structure determined by NMR in membrane-mimicking environments.
A kinked antimicrobial peptide from Bombina maxima. I. Three-dimensional structure determined by NMR in membrane-mimicking environments.
A kinked antimicrobial peptide from Bombina maxima. I. Three-dimensional structure determined by NMR in membrane-mimicking environments.
Eur Biophys J. 2011 Apr;40(4):447-62
Authors: Toke O, Bánóczi Z, Király P, Heinzmann R, Bürck J, Ulrich AS, Hudecz F
Maximin-4 is a 27-residue cationic antimicrobial peptide exhibiting selectivity for bacterial cells. As part of the innate defense system in the Chinese red-belly...
Oligomerization of the antimicrobial peptide Protegrin-5 in a membrane-mimicking environment. Structural studies by high-resolution NMR spectroscopy.
Linear Mode
