The widespread use of nanodiamond as a biomedical platform for drug-delivery, imaging, and subcellular tracking applications stems from its nontoxicity and unique quantum mechanical properties. Here, we extend this functionality to the domain of magnetic resonance, by demonstrating that the intrinsic electron spins on the nanodiamond surface can be used to hyperpolarize adsorbed liquid compounds at low fields and room temperature. By combining relaxation measurements with hyperpolarization, spins on the surface of the nanodiamond can be distinguished from those in the bulk liquid. These results are likely of use in signaling the controlled release of pharmaceutical payloads.
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Constant-variable flip angles for hyperpolarized media MRI #DNPNMR
From The DNP-NMR Blog:
Constant-variable flip angles for hyperpolarized media MRI #DNPNMR
Deng, H., et al., Constant-variable flip angles for hyperpolarized media MRI. J. Magn. Reson., 2016. 263: p. 92-100.
http://www.sciencedirect.com/science/article/pii/S1090780716000203
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06-21-2016 01:09 AM
Hyperpolarized Nanodiamond with Long Spin Relaxation Times
From The DNP-NMR Blog:
Hyperpolarized Nanodiamond with Long Spin Relaxation Times
Rej E, Gaebel T, Boele T, Waddington D, Reilly D. Hyperpolarized Nanodiamond with Long Spin Relaxation Times. ARXIV. 2015.
http://arxiv.org/abs/1502.06214
Structure of Peptides on Metal Oxide Surfaces Probed by NMR
Structure of Peptides on Metal Oxide Surfaces Probed by NMR
Peter A. Mirau, Rajesh R. Naik and Patricia Gehring
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja205454t/aop/images/medium/ja-2011-05454t_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/ja205454t
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/twbT3VIr8Xo
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10-22-2011 10:16 AM
[NMR paper] Identification of protein surfaces by NMR measurements with a pramagnetic Gd(III) che
Identification of protein surfaces by NMR measurements with a pramagnetic Gd(III) chelate.
Related Articles Identification of protein surfaces by NMR measurements with a pramagnetic Gd(III) chelate.
J Am Chem Soc. 2002 Jan 23;124(3):372-3
Authors: Pintacuda G, Otting G
Gd-diethylenetriamine pentaacetic acid-bismethylamide, Gd(DTPA-BMA), is shown to be a reagent suitable for the identification of protein surfaces. Compared to the conventionally used spin-label TEMPOL, Gd(DTPA-BMA) is a stronger relaxation agent, requiring lesser concentrations...
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11-24-2010 08:49 PM
[NMR paper] Exploring surfaces and cavities in lipoxygenase and other proteins by hyperpolarized
Exploring surfaces and cavities in lipoxygenase and other proteins by hyperpolarized xenon-129 NMR.
Related Articles Exploring surfaces and cavities in lipoxygenase and other proteins by hyperpolarized xenon-129 NMR.
J Am Chem Soc. 1999 Oct 13;121(40):9370-7
Authors: Bowers CR, Storhaug V, Webster CE, Bharatam J, Cottone A, Gianna R, Betsey K, Gaffney BJ
This paper presents an exploratory study of the binding interactions of xenon with the surface of several different proteins in the solution and solid states using both conventional and...
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11-18-2010 08:31 PM
[NMR paper] NMR identification of protein surfaces using paramagnetic probes.
NMR identification of protein surfaces using paramagnetic probes.
Related Articles NMR identification of protein surfaces using paramagnetic probes.
Biochemistry. 1990 Oct 30;29(43):10041-8
Authors: Petros AM, Mueller L, Kopple KD
Paramagnetic agents produce line broadening and thus cancellation of anti phase cross-peak components in two-dimensional correlated nuclear magnetic resonance spectra. The specificity of this effect was examined to determine its utility for identifying surface residues of proteins. Ubiquitin and hen egg white...
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08-21-2010 11:04 PM
[NMR paper] NMR studies of protein surfaces. The interaction of lysozyme with tri-N-acetylglucosa
NMR studies of protein surfaces. The interaction of lysozyme with tri-N-acetylglucosamine.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR studies of protein surfaces. The interaction of lysozyme with tri-N-acetylglucosamine.
Biochem Pharmacol. 1990 Jul 1;40(1):65-8
Authors: Petros AM, Kopple KD