[NMR paper] Dynamic membrane interactions of antibacterial and antifungal biomolecules, and amyloid peptides, revealed by solid-state NMR spectroscopy.
Related ArticlesDynamic membrane interactions of antibacterial and antifungal biomolecules, and amyloid peptides, revealed by solid-state NMR spectroscopy.
Biochim Biophys Acta. 2017 Jun 06;:
Authors: Naito A, Matsumori N, Ramamoorthy A
Abstract
A variety of biomolecules acting on the cell membrane folds into a biologically active structure in the membrane environment. It is, therefore, important to determine the structures and dynamics of such biomolecules in a membrane environment. While several biophysical techniques are used to obtain low-resolution information, solid-state NMR spectroscopy is one of the most powerful means for determining the structure and dynamics of membrane bound biomolecules such as antibacterial biomolecules and amyloidogenic proteins; unlike X-ray crystallography and solution NMR spectroscopy, applications of solid-state NMR spectroscopy are not limited by non-crystalline, non-soluble nature or molecular size of membrane-associated biomolecules. This review article focuses on the applications of solid-state NMR techniques to study a few selected antibacterial and amyloid peptides. Solid-state NMR studies revealing the membrane inserted bent ?-helical structure associated with the hemolytic activity of bee venom melittin and the chemical shift oscillation analysis used to determine the transmembrane structure (with ?-helix and 310-helix in the N- and C-termini, respectively) of antibiotic peptide alamethicin are discussed in detail. Oligomerization of an amyloidogenic islet amyloid polypeptide (IAPP, or also known as amylin) resulting from its aggregation in a membrane environment, molecular interactions of antifungal natural product amphotericin B with ergosterol in lipid bilayers, and mechanism of lipid raft formation by sphingomyelin studied using solid state NMR methods are also discussed in this review article. This article is part of a Special Issue entitled "Biophysical Exploration of Dynamical Ordering of Biomolecular Systems" edited by Dr. Koichi Kato.
PMID: 28599848 [PubMed - as supplied by publisher]
MembraneInsertion of a Dinuclear Polypyridylruthenium(II)Complex Revealed by Solid-State NMR and Molecular Dynamics Simulation:Implications for Selective Antibacterial Activity
MembraneInsertion of a Dinuclear Polypyridylruthenium(II)Complex Revealed by Solid-State NMR and Molecular Dynamics Simulation:Implications for Selective Antibacterial Activity
Daniel K. Weber, Marc-Antoine Sani, Matthew T. Downton, Frances Separovic, F. Richard Keene and J. Grant Collins
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.6b09996/20161109/images/medium/ja-2016-099965_0009.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.6b09996
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11-19-2016 08:35 PM
Structural Changes Associated with Transthyretin Misfoldingand Amyloid Formation Revealed by Solution and Solid-State NMR
Structural Changes Associated with Transthyretin Misfoldingand Amyloid Formation Revealed by Solution and Solid-State NMR
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00164/20160323/images/medium/bi-2016-00164v_0004.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00164
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03-24-2016 04:18 AM
[NMR paper] Structural Changes Associated with Transthyretin Misfolding and Amyloid Formation Revealed by Solution and Solid-State NMR.
Structural Changes Associated with Transthyretin Misfolding and Amyloid Formation Revealed by Solution and Solid-State NMR.
Structural Changes Associated with Transthyretin Misfolding and Amyloid Formation Revealed by Solution and Solid-State NMR.
Biochemistry. 2016 Mar 21;
Authors: Lim KH, Dasari AK, Hung I, Gan Z, Kelly JW, Wemmer DE
Abstract
Elucidation of structural changes involved in protein misfolding and amyloid formation is crucial for unraveling the molecular basis of amyloid formation. Here we report structural...
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03-22-2016 01:46 PM
[NMR paper] Membrane interactions of phylloseptin-1, -2, and -3 peptides by oriented solid-state NMR spectroscopy.
Membrane interactions of phylloseptin-1, -2, and -3 peptides by oriented solid-state NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif Related Articles Membrane interactions of phylloseptin-1, -2, and -3 peptides by oriented solid-state NMR spectroscopy.
Biophys J. 2014 Aug 19;107(4):901-11
Authors: Resende JM, Verly RM, Aisenbrey C, Cesar A, Bertani P, Piló-Veloso D, Bechinger B
Abstract
Phylloseptin-1, -2, and -3 are three members of the...
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04-23-2015 06:11 PM
Towards structure determination of self-assembled peptides using dynamic nuclear polarization enhanced solid-state NMR spectroscopy
From The DNP-NMR Blog:
Towards structure determination of self-assembled peptides using dynamic nuclear polarization enhanced solid-state NMR spectroscopy
Takahashi, H., et al., Towards structure determination of self-assembled peptides using dynamic nuclear polarization enhanced solid-state NMR spectroscopy. Angew Chem Int Ed Engl, 2013. 52(27): p. 6979-82.
http://www.ncbi.nlm.nih.gov/pubmed/23564735
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04-23-2014 06:31 PM
[NMR paper] The G-Protein-Coupled Neuropeptide Y Receptor Type 2 is Highly Dynamic in Lipid Membranes as Revealed by Solid-State NMR Spectroscopy.
The G-Protein-Coupled Neuropeptide Y Receptor Type 2 is Highly Dynamic in Lipid Membranes as Revealed by Solid-State NMR Spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles The G-Protein-Coupled Neuropeptide Y Receptor Type 2 is Highly Dynamic in Lipid Membranes as Revealed by Solid-State NMR Spectroscopy.
Chemistry. 2014 Mar 13;
Authors: Schmidt P, Thomas L, Müller P, Scheidt HA, Huster D
Abstract
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03-14-2014 07:34 PM
Towards Structure Determination of Self-Assembled Peptides Using Dynamic Nuclear Polarization Enhanced Solid-State NMR Spectroscopy
From The DNP-NMR Blog:
Towards Structure Determination of Self-Assembled Peptides Using Dynamic Nuclear Polarization Enhanced Solid-State NMR Spectroscopy
Takahashi, H., et al., Towards Structure Determination of Self-Assembled Peptides Using Dynamic Nuclear Polarization Enhanced Solid-State NMR Spectroscopy. Angew. Chem. Int. Ed., 2013: p. n/a-n/a.
http://www.ncbi.nlm.nih.gov/pubmed/23564735
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06-13-2013 04:24 AM
Solid-state NMR of amyloid membrane interactions.
Solid-state NMR of amyloid membrane interactions.
Solid-state NMR of amyloid membrane interactions.
Methods Mol Biol. 2011;752:165-77
Authors: Gehman JD, Separovic F
Solid-state NMR pulse sequences often feature fewer pulses and delays than the more common solution NMR experiments. This ostensible simplicity, however, belies the care with which experimental parameters must be determined, as solid-state NMR can be much less forgiving of improper experimental set-up. This is especially true of "semi-solid" samples, such as the phospholipid vesicles...
Dynamic membrane interactions of antibacterial and antifungal biomolecules, and amyloid peptides, revealed by solid-state NMR spectroscopy.
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