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CREATING PLATFORMS FOR THE PROTEOMICS AND MEMBRANE PROTEINS

Award Number: R01GM070622
ORGANIZATION: NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES
OPDIV: NIH
AWARD CLASS: DISCRETIONARY
AWARD ACTIVITY TYPE: SCIENTIFIC/HEALTH RESEARCH (INCLUDES SURVEYS)
PERIOD OF PERFORMANCE START DATE: 04/01/2004
PERIOD OF PERFORMANCE END DATE: 11/30/2013

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CREATING PLATFORMS FOR THE PROTEOMICS AND MEMBRANE PROTEINS - DESCRIPTION (provided by applicant): The long-term objective of this project is to design chromatographic methods for the isolation and identification of membrane proteins in order to aid in their proteomic analysis. Presently, membrane proteins are removed from their native biomembrane environment in order to perform electrophoretic separation in gels. This can be unsuitable due to protein aggregation. Indeed, membrane proteins are believed to be underrepresented as a fraction of the proteins that can be typically identified from cells in comparison with their soluble counterparts. To remedy this problem, membrane proteins and associated charged lipids will be separated by electrophoresis in solid supported lipid bilayers. This will maintain these biomacromolecules in a much more native like environment during the entire chromatographic procedure. Lipid bilayers represent a new material for separation and, therefore, it will be necessary to optimize the components of the bilayer which are employed as the separation matrix. Specifically, microdomain structures such as lipid rafts will be exploited in the process because of the differing ability of proteins to partition into liquid expanded and liquid condensed domains. In addition to membrane chemistry, the applied voltage, temperature, buffer conditions, and patterning processes will be tuned. It should also be possible to obtain two-dimensional separation. The second aim of this work is to develop supports that allow virtually all transmembrane proteins to remain laterally mobile within the planar bilayer environment. Transmembrane proteins, which protrude from the lower leaflet of the supported bilayer, can interact with an underlying inorganic support and become immobile. Two steps will be taken to remedy this problem. First, the bilayer will rest on a well-hydrated polymer cushion that will act to keep membrane proteins in an environment very close to the one found in lipid vesicles. Second, the polymer cushion will be decoupled from the substrate by a passivating protein film. The third aim of this proposal is to make the separated proteins available for interrogation by ion channel measurements. For this purpose, the isolated proteins bands will be interrogated over a glass nanopore electrode (GNE) approximately 100 to 500 nm in diameter. The final specific aim is to separate proteins from the inner membrane of E. coli. Particular attention will be paid to monitoring transmembrane species from the SEC and Tat translocation apparatuses. We will monitor the ion channel properties of these proteins. It will be necessary to ensure that all membrane proteins are highly vectorially oriented during the separation. PUBLIC HEALTH RELEVANCE: It is generally believed that 15 to 30% of open reading frames in the genomes of most organisms encode membrane proteins. Moreover, 2 out of 3 drug targets are proteins embedded in cellular membranes. It is therefore vital to develop chromatographic assays to identify these species, their expression levels, as well as follow posttranslational modifications.


Issue Date FY	Funding FY	Legal Entity Name	Legal Entity Address	Legal Entity City	Legal Entity State	Legal Entity Zip Code	Legal Entity COUNTY	Legal Entity COUNTRY	Assistance Listing	Award Code	Budget Year	Action Date	Action Type	Action Amount

Issue Date FY: 2013 ( Subtotal = $2,558 )
2013	2012	PENNSYLVANIA STATE UNIVERSITY	110 TECHNOLOGY CENTER BUILDING	UNIVERSITY PARK	PA	16802	CENTRE	USA	Biomedical Research and Research Training	001	9	3/27/2013	CHANGE OF GRANTEE / TRAINING INSTITUTION / AWARDING INSTITUTION	$129,564
2013	2012	TEXAS A & M RESEARCH FOUNDATION	400 Harvey Mitchell Parkway S,	COLLEGE STATION	TX	77845	BRAZOS	USA	Biomedical Research and Research Training	000	8	3/25/2013	NON-COMPETING CONTINUATION	-$127,006
														Subtotal = $2,558

Issue Date FY: 2012 ( Subtotal = $280,963 )
2012	2012	TEXAS A & M RESEARCH FOUNDATION	400 Harvey Mitchell Parkway S,	COLLEGE STATION	TX	77845	BRAZOS	USA	Biomedical Research and Research Training	001	8	3/26/2012	NON-COMPETING CONTINUATION	$28,096
2012	2012	TEXAS A & M RESEARCH FOUNDATION	400 Harvey Mitchell Parkway S,	COLLEGE STATION	TX	77845	BRAZOS	USA	Biomedical Research and Research Training	000	8	12/2/2011	NON-COMPETING CONTINUATION	$252,867
														Subtotal = $280,963

Issue Date FY: 2011 ( Subtotal = $280,963 )
2011	2011	TEXAS A & M RESEARCH FOUNDATION	400 Harvey Mitchell Parkway S,	COLLEGE STATION	TX	77845	BRAZOS	USA	Biomedical Research and Research Training	001	7	6/29/2011	NON-COMPETING CONTINUATION	$25,542
2011	2011	TEXAS A & M RESEARCH FOUNDATION	400 Harvey Mitchell Parkway S,	COLLEGE STATION	TX	77845	BRAZOS	USA	Biomedical Research and Research Training	000	7	12/1/2010	NON-COMPETING CONTINUATION	$255,421
														Subtotal = $280,963

Issue Date FY: 2010 ( Subtotal = $363,801 )
2010	2010	TEXAS A & M RESEARCH FOUNDATION	400 Harvey Mitchell Parkway S,	COLLEGE STATION	TX	77845	BRAZOS	USA	Trans-NIH Recovery Act Research Support	001	6	1/29/2010	SUPPLEMENT FOR EXPANSION	$80,000
2010	2010	TEXAS A & M RESEARCH FOUNDATION	400 Harvey Mitchell Parkway S,	COLLEGE STATION	TX	77845	BRAZOS	USA	Biomedical Research and Research Training	000	6	11/25/2009	NON-COMPETING CONTINUATION	$258,001
2010	2010	TEXAS A & M RESEARCH FOUNDATION	400 Harvey Mitchell Parkway S,	COLLEGE STATION	TX	77845	BRAZOS	USA	Biomedical Research and Research Training	002	6	5/12/2010	NON-COMPETING CONTINUATION	$25,800
														Subtotal = $363,801

Issue Date FY: 2009 ( Subtotal = $298,293 )
2009	2009	TEXAS A & M RESEARCH FOUNDATION	400 Harvey Mitchell Parkway S,	COLLEGE STATION	TX	77845	BRAZOS	USA	Biomedical Research and Research Training	001	5	11/24/2008	COMPETING CONTINUATION	$298,293
2009	2007	TEXAS A & M UNIVERSITY RESEARCH FOUNDATION	400 Harvey Mitchell Parkway S,	COLLEGE STATION	TX	77845	BRAZOS	USA	Biomedical Research and Research Training	000	4	11/24/2008	NON-COMPETING CONTINUATION	$0
														Subtotal = $298,293

Issue Date FY: 2007 ( Subtotal = $228,080 )
2007	2007	TEXAS A & M UNIVERSITY RESEARCH FOUNDATION	POST OFFICE BOX 3578	COLLEGE STATION	TX	77843	BRAZOS	USA	Biomedical Research and Research Training	000	4	3/29/2007	NON-COMPETING CONTINUATION	$228,080
														Subtotal = $228,080

Issue Date FY: 2006 ( Subtotal = $234,892 )
2006	2006	TEXAS A & M UNIVERSITY RESEARCH FOUNDATION	POST OFFICE BOX 3578	COLLEGE STATION	TX	77843	BRAZOS	USA	Biomedical Research and Research Training	000	3	5/1/2006	NON-COMPETING CONTINUATION	$234,892
														Subtotal = $234,892

Issue Date FY: 2005 ( Subtotal = $288,842 )
2005	2005	TEXAS A & M UNIVERSITY RESEARCH FOUNDATION	POST OFFICE BOX 3578	COLLEGE STATION	TX	77843	BRAZOS	USA	Biomedical Research and Research Training	000	2	3/25/2005	NON-COMPETING CONTINUATION	$288,842
														Subtotal = $288,842

Issue Date FY: 2004 ( Subtotal = $277,925 )
2004	2004	TEXAS A & M UNIVERSITY RESEARCH FOUNDATION	POST OFFICE BOX 3578	COLLEGE STATION	TX	77843	BRAZOS	USA	Biomedical Research and Research Training	000	1	3/15/2004	NEW	$250,497
2004	2004	TEXAS A & M UNIVERSITY RESEARCH FOUNDATION	POST OFFICE BOX 3578	COLLEGE STATION	TX	77843	BRAZOS	USA	Biomedical Research and Research Training	001	1	9/13/2004	SUPPLEMENT FOR EXPANSION	$27,428
														Subtotal = $277,925

Grand Total All Awards = $2,256,317

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CREATING PLATFORMS FOR THE PROTEOMICS AND MEMBRANE PROTEINS

Award Number: R01GM070622

ORGANIZATION: NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES

OPDIV: NIH

AWARD CLASS: DISCRETIONARY

AWARD ACTIVITY TYPE: SCIENTIFIC/HEALTH RESEARCH (INCLUDES SURVEYS)

PERIOD OF PERFORMANCE START DATE: 04/01/2004

PERIOD OF PERFORMANCE END DATE: 11/30/2013

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