This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. Both normal and cancerous cells will be incubated in the presence of PTM-TE probe, after which the cells will be recovered, washed, and re-suspended in fresh culture medium. The cells will be placed in a flat cell-culture type sample container, as recommended by ACERT personnel, placed in the ESR microscopy unit, and ESRM images of individual cells will be obtained. Localization of spin density will be determined within the sub-cellular compartments. These experiments will allow us to determine whether or not cellular uptake of the probes will result in diffuse concentration within the cells, or whether the PTM-TE probe localizes to a particular subcellular location. If this is found to be the case, it may then be possible to modify the molecules so as to direct specific sub-cellular targeting by the probes. We are developing and characterizing LiNc-BuO and other particulate spin-probes that are embedded in a biocompatible and oxygen-permeable polymeric material. As an extension of these efforts, we propose to use the trityl molecular probes PTM-TE and PTM-TC as dopants for oxygen-permeable polymeric materials, including polydimethylsiloxane (PDMS) and silk fibroin. PDMS doped with PTM-TE has been developed in our lab, and these probes are commonly referred to as """"""""SpinChips."""""""" We shall use the ESRM capability of ACERT to assist in determining the optimal doping concentration for use with these materials. ESRM will permit us to determine the degree of aggregation of the trityl molecules that may result in spin-spin interaction and artificial line-broadening of the signal obtained - a concern that should be avoided.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
2P41RR016292-11
Application #
8364105
Study Section
Special Emphasis Panel (ZRG1-BCMB-K (40))
Project Start
2011-09-01
Project End
2012-08-31
Budget Start
2011-09-01
Budget End
2012-08-31
Support Year
11
Fiscal Year
2011
Total Cost
$482
Indirect Cost
Name
Cornell University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
872612445
City
Ithaca
State
NY
Country
United States
Zip Code
14850
Jain, Rinku; Vanamee, Eva S; Dzikovski, Boris G et al. (2014) An iron-sulfur cluster in the polymerase domain of yeast DNA polymerase ?. J Mol Biol 426:301-8
Pratt, Ashley J; Shin, David S; Merz, Gregory E et al. (2014) Aggregation propensities of superoxide dismutase G93 hotspot mutants mirror ALS clinical phenotypes. Proc Natl Acad Sci U S A 111:E4568-76
Georgieva, Elka R; Borbat, Peter P; Ginter, Christopher et al. (2013) Conformational ensemble of the sodium-coupled aspartate transporter. Nat Struct Mol Biol 20:215-21
Airola, Michael V; Sukomon, Nattakan; Samanta, Dipanjan et al. (2013) HAMP domain conformers that propagate opposite signals in bacterial chemoreceptors. PLoS Biol 11:e1001479
Airola, Michael V; Huh, Doowon; Sukomon, Nattakan et al. (2013) Architecture of the soluble receptor Aer2 indicates an in-line mechanism for PAS and HAMP domain signaling. J Mol Biol 425:886-901
Sun, Yan; Zhang, Ziwei; Grigoryants, Vladimir M et al. (2012) The internal dynamics of mini c TAR DNA probed by electron paramagnetic resonance of nitroxide spin-labels at the lower stem, the loop, and the bulge. Biochemistry 51:8530-41
Yu, Renyuan Pony; Darmon, Jonathan M; Hoyt, Jordan M et al. (2012) High-Activity Iron Catalysts for the Hydrogenation of Hindered, Unfunctionalized Alkenes. ACS Catal 2:1760-1764
Dzikovski, Boris; Tipikin, Dmitriy; Freed, Jack (2012) Conformational distributions and hydrogen bonding in gel and frozen lipid bilayers: a high frequency spin-label ESR study. J Phys Chem B 116:6694-706
Gaffney, Betty J; Bradshaw, Miles D; Frausto, Stephen D et al. (2012) Locating a lipid at the portal to the lipoxygenase active site. Biophys J 103:2134-44
Maeda, Kiminori; Lodge, Matthew T J; Harmer, Jeffrey et al. (2012) Electron tunneling in lithium-ammonia solutions probed by frequency-dependent electron spin relaxation studies. J Am Chem Soc 134:9209-18

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