Funding Opportunities

PROGRAM DESCRIPTION
“Subcellular Resolution Probes of Apoptotic Protein Assembly in Mitochondrial Pore Formation”
Nanoscale Interdisciplinary Research Teams (NIRT)
National Science Foundation
Application submission date: November 12, 2004

PROGRAM DESCRIPTION
“Technology Development to Measure Dynamics of Protein Function and Interaction”
National Technology Center for Networks and Pathways
National Institute of Health, RFA-RM-04-019
Application submission date: February 22, 2005

PROGRAM DESCRIPTION
The objective of the program is to make available to institutions expensive research instruments that can only be justified on a shared use basis and for which meritorious research projects are described. The SIG program provides a cost effective mechanism for groups of NIH supported investigators to obtain commercially available technologically sophisticated equipment costing more than $100,000.

Types of instrumentation supported include, but are not limited to nuclear magnetic resonance systems, electron and confocal microscopes, mass spectrometers, protein and DNA sequencers, biosensors, x-ray diffractometers and cell sorters.

A major user group of three or more investigators must be identified. A minimum of three major users must be Principal Investigators on NIH peer reviewed research grants at the time of the application and award.

National Institute of Neurological Disorders and Stroke (NINDS)
http://www.ninds.nih.gov
INSTITUTIONAL CENTER CORE GRANT TO SUPPORT NEUROSCIENCE RESEARCH
RELEASE DATE: February 11, 2002
PA NUMBER: PAR-02-059
EXPIRATION DATE: February 28, 2005, unless reissued.

PROGRAM DESCRIPTION
“Molecular and Structural Mechanisms, Detection and Antagonism of Anthrax Toxin”
National Institute of Allergy and Infectious Diseases
Application submission date: June 1, 2005

PROGRAM DESCRIPTION
Each Center Core Grant will support shared resources and facilities used by investigators with research projects funded by NINDS. This support, by providing more accessible resources, is expected to assure a greater productivity than would be possible from the separate projects. An institution is eligible for a maximum of one NINDS Center Core Grant. These awards will support basic, translational, and clinical research, but will not be used to support clinical trials or to provide patient services.

National Institute of Allergy and Infectious Diseases (NIAID)
http://www.niaid.nih.gov
BIODEFENSE AND EMERGING INFECTIOUS DISEASES RESEARCH OPPORTUNITIES
PA NUMBER: PA-03-080

Application Types and Standard Receipt Dates: R21, R01, and P01

PROGRAM DESCRIPTION
Responsive applications should specifically address NIAID Category A, B and C Priority Pathogens, their toxic products, the diseases caused by them, and/or relevant host immune responses.
The current list of pathogens is available at: http://www.niaid.nih.gov/biodefense/bandc_priority.htm. Although the SARS coronavirus is not listed as a biodefense priority pathogen, NIAID has amended Program Announcement PA-03-080 to include support for basic research on SARS as an emerging infectious disease.

While the long-term public health significance of SARS is not known, its recent emergence, ease of transmission, and disease severity warrants an immediate response from the biomedical research community. NIAID is soliciting applications for research on SARS that include, but are not limited to, the following highlighted research areas: the role of co-infection with other respiratory pathogens, the significance of viral persistence, the presence of debilitating diseases, the role of genetic and non-genetic risk factors, elucidation of protective immunity, and identification of SARS virulence factors and host responses associated with lung pathology.

In some cases, immunological mechanisms relevant to biodefense are broadly applicable for many pathogens and may be most efficiently studied using model systems. Immunological research that is not directed specifically at NIAID Category A, B and C Priority Pathogens or their products is responsive if it addresses a practical approach to inducing, controlling or improving the effectiveness of innate or adaptive immune responses to infection by those pathogens or vaccines to prevent them. Responsive applications may also address basic immunological mechanisms when understanding those mechanisms is necessary for the development of protective approaches for biodefense.

Interdisciplinary groups that address crosscutting, connected research questions important to the eventual development of control measures for infectious agents with bioterrorism potential are encouraged to apply.

Department of Defense
Homeland Security Advanced Research Projects Agency (HSARPA)
http://www.acq.osd.mil/sadbu/sbir/othersites/index.htm
Detection Systems for Biological and Chemical Countermeasures
National Institute of General Medical Sciences (NIGMS), the National Institute of Biomedical Imaging and Bioengineering (NIBIB), and the National Human Genome research Institute (NHGRI)
P20 Exploratory Center Grants
PROGRAM DESCRIPTION
Development of High Resolution Probes for Cellular Imaging

Defense Advanced Research Projects Agency (DARPA)
http://www.darpa.mil/baa/
PROGRAM DESCRIPTION
Technical topic areas of interest to DSO
New materials, materials concepts, materials processing and devices
Advanced Mathematics
Biological Warfare Defense
Applications of biology to defense applications

Call for Participation and Use of the Neuroproteomics Cores Center P30

Dear Colleagues,

We are planning to submit an application for a Neuroproteomics Resource Center P30 Grant for a June 1 deadline. This application responds to the announcement NINDS Institutional Center Core Grants to Support Neuroscience Research (PAR-02-059), http://grants.nih.gov/grants/guide/pa-files/PAR-02-059.html. The primary mission of this type of P30 Grant is to support the research of NINDS-funded and other NIH-funded neuroscience projects. The funds obtained by the P30 grant will be used to purchase and maintain new instrumentation for the Cores, to support technical experts to operate the Cores and to purchase supplies for utilization of the core resources by participating faculty. We believe this Cores Resource will strengthen Neuroscience research in the Drexel Community and greatly expand your chances to obtain additional research grant funding. The Neuroscience area of research at Drexel already is high quality, at a level which is well-positioned to utilize and gain from a Proteomics Cores Center. It also will help stimulate the overall development of proteomics-based sciences in our Community. The Cores that are being established will include the following.

Proteome Mapping Core
Molecular Resources Core
Protein Interactions Core
Protein Spatial Mapping Core

A description of the services envisioned for the Cores is attached and also given below.

At this stage, we need to identify all in the Neuroscience community who will utilize the P30 Resource and to include your science and administrative information in the application. We invite you to participate. If you wish to do so, please inform us as soon as possible. We will need the following materials.

Immediately: Expression of interest

April 16th: One page summary of your NIH-funded research, including title, grant number(s), abstract, and strong statements on how you will use the Cores (any or all). Human subjects: IRB # and approval date. Animal subjects: IACUC Protocol # and approval date.

April 23th: NIH biosketch (4 page) and a separate NIH-formatted Other Support document.

If you have any questions about this initiative, please contact Noreen Robertson (nmr26@drexel.edu) or Irwin Chaiken (imc23@drexel.edu).

Please send responses and materials to cps33@drexel.edu.

Neuroproteomics Cores Center

Proteome Mapping Core (Manjappara, Robertson). This Core will provide the Ciphergen ProteinChip® Biology System and an operator. This will enable users to investigate three major types of protein analysis.

• Global mass spectral proteome maps for biological samples such as cells and tissues.
Determine proteomic changes in response to specific stimuli, with the ability to analyze trace (low femtomole) analytes from samples including cell/tissue lysates, immunoprecipitates and laser-captured samples. Generate differential protein expression maps.
• Develop purification strategies for specific proteins identified in the global maps.
Identification of proteins captured by a particular set of chip surfaces can lead to corresponding chromatographic media to purify proteins of interest. The final definition of exact mass and structure, will have access to high end mass spectrometry at CHOP.
• Mapping of protein interaction networks and posttranslational modifications.
Identification of new binding interactants and interaction networks. Using antibodies, isolated proteins, oligonucleotides or other biological molecules as chip-immobilized ligands, proteins captured on the chip surface from biological samples can be identified. Proteins can be further processed on chip, via peptide mapping, epitope mapping, enzymatic analysis of post-translational modifications (glycosylation/phosphorylation analysis) or protein interaction studies (protein-protein interaction, receptor-ligand interaction, DNA-protein interaction).

Molecular Resources Core (Scibek, Saunders, Robertson). This core will provide resources for the synthesis of peptides, access to monoclonal antibodies (being explored), construction of expression vectors and cells and production of proteins.
• Molecular cloning of target proteins
Source to clone target proteins into appropriate expression vectors
• Expression of recombinant target proteins
Infrastructure exists to express recombinant proteins in mammalian, insect and bacterial systems.
• Purification of recombinant proteins
Recombinant proteins will be purified using standard chromatographic techniques including FPLC and HPLC.
• Peptide synthesis and purification
Applied Biosystem 433A peptide synthesizer will be used to generate peptides for identification and quantification of peptides obtained following trypsin cleavage of target proteins.
Protein Interactions Core (Cocklin, Ishino, Saunders). The Interactions Core will provide both access to a BIA3000 SPR optical biosensor and experienced operators. The Core also will provide access to yeast-2-hybrid analysis of protein interactions.
• Simple macromolecular interactions. BIA3000 monitoring of simple interactions between two biomolecules e.g., protein-protein, protein-peptide, protein-carbohydrate, protein-DNA, protein-RNA interactions, including the derivation of individual and equilibrium kinetic constants.
• Real Time Formation of Multimolecular Complexes. The BIA3000 biosensor can qualitatively monitor the successive interactions of many individual molecules upon a base ligand e.g., the formation of multiple transcription factors upon each other and/or on promoter DNA, etc.
• Biosensing in a Membrane-like environment. Biosensor methodologies now exist that allow interactions to be probed within the context of a model membrane, e.g., (i) (peptide/protein/carbohydrate) membrane interactions, and (ii) the interactions of peptides/protein/carbohydrates with protein embedded with a model membrane.

Protein Spatial Mapping Core (Nissanov and Rioux).
• Laser capture microscopy
• Immunodetection amplified with T7 RNA polymerase
A fundamental constraint of immunohistochemical methods for localizing protein is their qualitative rather than quantitative nature and their failure to simultaneously differentiate a large number of molecular moieties. By combining laser capture microscopy (LCM) and immunodetection amplified with T7 RNA polymerase (IDAT), these shortcomings will be overcome. Cells or regions could be collected by microdissection guided by a counterstain stain, a subsidiary label, or a reporter protein. The material will then be subjected to IDAT analysis to yield absolute protein level for multiple proteins in the given sample. IDAT is exquisitely sensitive and can be used for quantification of proteins in a single cell. By mapping the results back on to the sectional material, accurate expression profiles can be constructed. When a full 3D mapping is required, for example when protein expression is to be assessed as a function of position relative to say an injury site, an additional technology- - cryoplane microscopy (CM)`- will be brought to bear. This new imaging modality supports 3D fluorescent and brightfield imaging during production of sectional material. With the aid of available registration technology, the sectional material, along with the IDAT generated profile, can be mapped back onto the 3D tissue. The Core will provide the needed instrumentation and its staff will be available to run 3D imaging sessions, design and implement automated LCM protocols, and perform IDAT analysis using user provided primary antibodies for the proteins of interest.