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 ?-sheet. But despite the wealth of data available today, protegrin dimer structure and pore formation is still not completely understood. In order to investigate a more detailed dimerization process of PG-1 and if it will be the same for another type of protegrins, in this work we used a high-resolution NMR spectroscopy for structure determination of protegrin-3 (RGGGL-CYCRR-RFCVC-VGR) in the presence of perdeuterated DPC micelles and demonstrate that PG-3 forms an antiparallel NCCN dimer with a possible association of these dimers. This structural study complements previously published solution, solid state and computational studies of PG-1 in various environments and validate the potential of mean force simulations of PG-1 dimers and association of dimers to form octameric or decameric ?-barrels.
[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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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 study of the structure and self-association of Core peptide in aqueous solution and DPC micelles.
NMR study of the structure and self-association of Core peptide in aqueous solution and DPC micelles.
NMR study of the structure and self-association of Core peptide in aqueous solution and DPC micelles.
Biopolymers. 2011;96(2):177-80
Authors: Zheng G, Torres AM, Ali M, Manolios N, Price WS
Core peptide is a hydrophobic peptide derived from the T-cell antigen receptor-alpha chain (TCR-alpha) transmembrane region with therapeutic potential. The mechanism by which the peptide inserts into the membrane, including any requirements to change...
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07-20-2011 10:00 AM
[NMR paper] High-resolution molecular structure of a peptide in an amyloid fibril determined by m
High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy.
Related Articles High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy.
Proc Natl Acad Sci U S A. 2004 Jan 20;101(3):711-6
Authors: Jaroniec CP, MacPhee CE, Bajaj VS, McMahon MT, Dobson CM, Griffin RG
Amyloid fibrils are self-assembled filamentous structures associated with protein deposition conditions including Alzheimer's disease and the transmissible...
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11-24-2010 09:25 PM
[NMR paper] High-resolution NMR study of a synthetic oligoribonucleotide with a tetranucleotide G
High-resolution NMR study of a synthetic oligoribonucleotide with a tetranucleotide GAGA loop that is a substrate for the cytotoxic protein, ricin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles High-resolution NMR study of a synthetic oligoribonucleotide with a tetranucleotide GAGA loop that is a substrate for the cytotoxic protein, ricin.
Nucleic Acids Res. 1993 Dec 11;21(24):5670-8
Authors: Orita M, Nishikawa F, Shimayama T, Taira K, Endo Y, Nishikawa S
...
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[NMR paper] High-resolution NMR study of the pressure-induced unfolding of lysozyme.
High-resolution NMR study of the pressure-induced unfolding of lysozyme.
Related Articles High-resolution NMR study of the pressure-induced unfolding of lysozyme.
Biochemistry. 1992 Sep 1;31(34):7773-8
Authors: Samarasinghe SD, Campbell DM, Jonas A, Jonas J
The pressure-induced reversible unfolding of lysozyme was investigated by high-resolution proton magnetic resonance spectroscopy by following the proton spectra of the following residues: His-15 epsilon 1, Trp-28 epsilon 3, Leu-17 delta 2, Cys-64 alpha, and Trp-108 epsilon 3. The...
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08-21-2010 11:45 PM
[NMR paper] High-resolution 13C NMR study of the topography and dynamics of methionine residues i
High-resolution 13C NMR study of the topography and dynamics of methionine residues in detergent-solubilized bacteriorhodopsin.
Related Articles High-resolution 13C NMR study of the topography and dynamics of methionine residues in detergent-solubilized bacteriorhodopsin.
Biochemistry. 1991 Apr 23;30(16):3885-92
Authors: Seigneuret M, Neumann JM, Levy D, Rigaud JL
The proton transport membrane protein bacteriorhodopsin has been biosynthetically labeled with methionine and studied by high-resolution 13C NMR after solubilization in the detergent...
Antimicrobial peptide protegrin-3 adopt an antiparallel dimer in the presence of DPC micelles: a high-resolution NMR study.
Linear Mode
