[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 against multidrug resistant bacterial pathogens. Thanatin, an insect derived pathogen inducible 21-residue long antimicrobial peptide, demonstrates antimicrobial activity toward broad range of pathogens. Thanatin is an excellent candidate for antibiotics development due to potent in vivo activity in animal model and low toxicity to human cells. Recent studies indicated mode of action of thanatin could be intriguing and may comprise bacterial membrane permeabilization and interactions with periplasmic proteins. In order to better understand selectivity and membrane disruption, here, we determined 3-D structure of the thanatin in zwitterionic DPC-d38 micelle by NMR spectroscopy. The depth of insertion of thanatin into micelle structure was investigated by spin labelled doxyl lipids, 5-DSA and 16-DSA. DPC-bound structure of thanatin is defined by a ?-hairpin structure and an extended and turn conformations, for residues G1-I8, at the N-terminus. The ?-hairpin structure is delineated by two antiparallel ?-strands, residues I9-C11 and residues K17-R20, which is connected by loop consisted of residues N12-G16. There are cross ?-strands sidechain-sidechain packing interactions among hydrophobic and aromatic residues. Spin labelled lipid studies revealed a set of spatially proximal residues V6, I8, Q19, R20 and M21 may be deeply inserted into the hydrophobic core of the DPC micelle. While, residues including those at the turn/loop are merely surface localized. The atomic resolution structure and orientation of thanatin in zwitterionic DPC micelle may be utilized for understating mode of action in lipid membrane and further development of non-toxic analogs.
PMID: 32781154 [PubMed - as supplied by publisher]
[NMR paper] Metal-ion Binding to Host Defense Peptide Piscidin 3 Observed in Phospholipid Bilayers by Magic Angle Spinning Solid-state NMR.
Metal-ion Binding to Host Defense Peptide Piscidin 3 Observed in Phospholipid Bilayers by Magic Angle Spinning Solid-state NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-7315-19-Wiley_FullText_120x30_orange.png Related Articles Metal-ion Binding to Host Defense Peptide Piscidin 3 Observed in Phospholipid Bilayers by Magic Angle Spinning Solid-state NMR.
Chemphyschem. 2019 01 21;20(2):295-301
Authors: Rai RK, De Angelis A, Greenwood A, Opella SJ, Cotten ML
Abstract
Cationic...
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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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[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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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
Antimicrobial peptides and their superior fluorinated analogues: structure-activity relationships as revealed by NMR spectroscopy and MD calculations.
Antimicrobial peptides and their superior fluorinated analogues: structure-activity relationships as revealed by NMR spectroscopy and MD calculations.
Antimicrobial peptides and their superior fluorinated analogues: structure-activity relationships as revealed by NMR spectroscopy and MD calculations.
Chembiochem. 2010 Nov 22;11(17):2424-32
Authors: Díaz MD, Palomino-Schätzlein M, Corzana F, Andreu C, Carbajo RJ, del Olmo M, Canales-Mayordomo A, Pineda-Lucena A, Asensio G, Jiménez-Barbero J
The conformations of two synthetic pentapeptides with...
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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...
NMR structure and localization of the host defense antimicrobial peptide thanatin in zwitterionic dodecylphosphocholine micelle: Implications in antimicrobial activity.
Linear Mode
