Grant List
Represents Grant table in the DB
GET /v1/grants?page%5Bnumber%5D=1393&sort=abstract
{ "links": { "first": "https://cic-apps.datascience.columbia.edu/v1/grants?page%5Bnumber%5D=1&sort=abstract", "last": "https://cic-apps.datascience.columbia.edu/v1/grants?page%5Bnumber%5D=1405&sort=abstract", "next": "https://cic-apps.datascience.columbia.edu/v1/grants?page%5Bnumber%5D=1394&sort=abstract", "prev": "https://cic-apps.datascience.columbia.edu/v1/grants?page%5Bnumber%5D=1392&sort=abstract" }, "data": [ { "type": "Grant", "id": "7326", "attributes": { "award_id": "3U45ES006155-30S1", "title": "AFC Hazardous Materials Worker Training", "funder": { "id": 4, "ror": "https://ror.org/01cwqze88", "name": "National Institutes of Health", "approved": true }, "funder_divisions": [ "National Institute of Environmental Health Sciences (NIEHS)" ], "program_reference_codes": [], "program_officials": [ { "id": 21583, "first_name": "Demia", "last_name": "Wright", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [] } ], "start_date": "1992-09-16", "end_date": "2021-05-31", "award_amount": 150000, "principal_investigator": { "id": 23114, "first_name": "Kenneth", "last_name": "Oldfield", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [ { "id": 1569, "ror": "", "name": "ALABAMA FIRE COLLEGE", "address": "", "city": "", "state": "AL", "zip": "", "country": "United States", "approved": true } ] }, "other_investigators": [], "awardee_organization": { "id": 1569, "ror": "", "name": "ALABAMA FIRE COLLEGE", "address": "", "city": "", "state": "AL", "zip": "", "country": "United States", "approved": true }, "abstract": "With this application, the Alabama Fire College (AFC) requests supplemental funding to conduct COVID-19 specific health and safety training with public safety personnel, including healthcare workers and others that are considered essential workers during the COVID-19 response. Using current Bureau of Labor Statistics, there are over 556,000 public safety and healthcare personnel working in the region including those who will provide patient transport or are members of emergency response teams and have roles which will require them to respond to an infectious disease outbreak such as the COVID-19 pandemic. Most of these personnel work in rural areas or medically underserved areas which put them and the patients they serve at greater risk. All these target populations have in common the potential for exposure to persons infected with COVID-19 and other emerging infectious diseases, through direct contact with infected individuals as well as through surface contamination or other contaminated materials. Alabama and Mississippi contain many medically underserved areas, health professional shortage areas, health department with limited budgets and limited ability to conduct contact tracing, and limited access to professional occupational safety and health training programs. Unfortunately, federal funds for preparedness assistance have not reached public safety and healthcare professionals in the amounts sufficient to meet their needs for training. AFC and it’s partner, UAB, will develop and implement evidence-based training tools that are locally-relevant and consistent with the NIEHS WTP Coronavirus Bio-safety Initiative and guidance from the Centers for Disease Control and Prevention (CDC), the Occupational Safety and Health Administration (OSHA), the National Institute for Occupational Safety and Health (NIOSH), as well as other recognized health professionals. The proposed project will bring critical training to over 400 participants in webinar, virtual simulation, YouTube video, and limited in-person training. Courses will also be available through AFC’s learning management system to Native American tribes and other responders and essential workers, adding many potential trainees through distance education.", "keywords": [ "Address", "Air", "Alabama", "Area", "Budgets", "Bureau of Indian Affairs", "COVID-19", "COVID-19 pandemic", "Centers for Disease Control and Prevention (U.S.)", "Chemicals", "Communicable Diseases", "Communities", "Confined Spaces", "Contact Tracing", "Coronavirus", "Disasters", "Disease Outbreaks", "Distance Education", "Emergency Medical Technicians", "Emergency response", "Emerging Communicable Diseases", "Employee", "Employment", "Environment", "Event", "Exposure to", "Face", "Fire - disasters", "Fishes", "Florida", "Funding", "Goals", "Hazardous Substances", "Hazardous Waste", "Health", "Health Personnel", "Health Professional", "Human Resources", "Individual", "Law Enforcement", "Learning", "Location", "Louisiana", "Measures", "Medical", "Medically Underserved Area", "Mississippi", "Modeling", "National Institute for Occupational Safety and Health", "National Institute of Environmental Health Sciences", "Native Americans", "North Carolina", "Occupational", "Occupational Health", "Occupational Safety", "Occupations", "Paramedical Personnel", "Participant", "Patient Care", "Patients", "Persons", "Police", "Population", "Public Health", "Readiness", "Risk", "Role", "Safety", "Schedule", "Societies", "Surface", "System", "Target Populations", "Tennessee", "Terrorism", "Trainers Training", "Training", "Training Programs", "Triage", "Tribes", "United States Occupational Safety and Health Administration", "Universities", "Work", "Workplace", "college", "evidence base", "hazard", "hazardous materials disaster", "health professional shortage areas", "medical schools", "member", "outreach", "peer", "peer support", "programs", "response", "rural area", "severe weather", "statistics", "tool", "tribal member", "virtual reality simulation", "volunteer", "webinar" ], "approved": true } }, { "type": "Grant", "id": "4298", "attributes": { "award_id": "1625792", "title": "MRI: Acquisition of X-Ray Photoelectron Spectrometer for Discovering New Phenomena with In Situ Studies", "funder": { "id": 3, "ror": "https://ror.org/021nxhr62", "name": "National Science Foundation", "approved": true }, "funder_divisions": [ "Mathematical and Physical Sciences (MPS)", "Major Research Instrumentation" ], "program_reference_codes": [], "program_officials": [ { "id": 14593, "first_name": "Carlos", "last_name": "Murillo", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [] } ], "start_date": "2016-09-15", "end_date": "2020-08-31", "award_amount": 699300, "principal_investigator": { "id": 14598, "first_name": "Lawrence", "last_name": "Baker", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [ { "id": 308, "ror": "", "name": "Ohio State University", "address": "", "city": "", "state": "OH", "zip": "", "country": "United States", "approved": true } ] }, "other_investigators": [ { "id": 14594, "first_name": "Umit S", "last_name": "Ozkan", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [] }, { "id": 14595, "first_name": "Gerald S", "last_name": "Frankel", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [] }, { "id": 14596, "first_name": "Anne", "last_name": "Co", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [] }, { "id": 14597, "first_name": "David", "last_name": "Cole", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [] } ], "awardee_organization": { "id": 308, "ror": "", "name": "Ohio State University", "address": "", "city": "", "state": "OH", "zip": "", "country": "United States", "approved": true }, "abstract": "With this award from the Major Research Instrumentation (MRI) and Chemistry Research Instrumentation and Facilities (CRIF) Programs, Professor L. Robert Baker from Ohio State University (OSU) and colleagues Umit Ozkan, Gerald Frankel, Anne Co and David Cole have acquired an X-ray photoelectron spectrometer (XPS) which operates at near ambient pressures instead of the more usual high-vacuum operation of standard XPS. These instruments use X-rays to eject electrons from surfaces. The electrons are detected and analyzed to identify the elemental and chemical composition of such surfaces. This surface-sensitive probe is used to study electronic devices, batteries, fuel cells, sensors, corrosion, materials degradation, catalytic reactions and geochemistry. It serves the need in academia and industry to probe chemical details of solid and liquid surfaces under chemically-relevant conditions. The instrument is used by researchers at OSU and about a dozen regional institutions including industries and institutions serving underrepresented minorities in STEM fields. This participation generates a significant regional impact. Undergraduate and graduate students are trained to use the instrument in research projects, laboratory coursework and workshops. \n\nThe award is aimed at enhancing research and education at all levels at OSU, especially in areas such as: (a) studying solid electrolyte interphase and interfacial ion solvation, (b) probing catalysis, electrocatalysis, and solid oxide fuel cells, (c) analyzing materials degradation and corrosion, and (d) studying earth science and geochemistry.", "keywords": [], "approved": true } }, { "type": "Grant", "id": "4551", "attributes": { "award_id": "1465180", "title": "Quasi-free electron energy in supercritical carbon dioxide and water: A research program involving rural and first-generation STEM students", "funder": { "id": 3, "ror": "https://ror.org/021nxhr62", "name": "National Science Foundation", "approved": true }, "funder_divisions": [ "Mathematical and Physical Sciences (MPS)", "Chem Struct,Dynmcs&Mechansms A" ], "program_reference_codes": [], "program_officials": [ { "id": 15682, "first_name": "Rebecca", "last_name": "Peebles", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [] } ], "start_date": "2015-09-01", "end_date": "2020-08-31", "award_amount": 395000, "principal_investigator": { "id": 15684, "first_name": "Cherice", "last_name": "Evans", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [ { "id": 722, "ror": "", "name": "CUNY Queens College", "address": "", "city": "", "state": "NY", "zip": "", "country": "United States", "approved": true } ] }, "other_investigators": [ { "id": 15683, "first_name": "Gary L", "last_name": "Findley", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [] } ], "awardee_organization": { "id": 722, "ror": "", "name": "CUNY Queens College", "address": "", "city": "", "state": "NY", "zip": "", "country": "United States", "approved": true }, "abstract": "With this award, the Chemical Structure, Dynamics, and Mechanisms (CSDM-A) Program of the Division of Chemistry is supporting Professor Cherice M. Evans at CUNY - Queens College and Professor Gary L. Findley at the University of Louisiana-Monroe to undertake complementary experimental and theoretical studies of the role of solvent structure in important chemical reactions. Their work seeks improved understanding upon which to base better, more efficient, and less environmentally invasive chemical manufacturing and processing. It is congruent with the aims of sustainable chemistry, including the principles that the use of solvents should be made unnecessary wherever possible, and solvents should be innocuous when used. By involving graduate and undergraduate students from CUNY as well as undergraduates from Louisiana - Monroe (many of whom are from low-income families and are first generation college students), the work makes available exciting research opportunities intended not only to advance science, but to retain student interest and expand capabilities in STEM fields. Some of the research utilizes synchrotron facilities at the Center for Advanced Microstructures and Devices in Baton Rouge, LA, allowing all participating students to interact with scientists from a high caliber user facility, while introducing CUNY students to new aspects of United States culture in a Living/Learning community environment. The requirement that Monroe participants present their research results at Queens College ensures that these students will be exposed to a major urban environment -a first for many of these students.\n\nThe research specifically focuses on solvation of quasi-free electrons as probes of the solvent structure in the target media across the broad temperature and density range represented by these solvents. The systems chosen for study include supercritical carbon dioxide, high temperature water, and supercritical water. These solvents are targeted because their solvation properties can be adjusted by small changes in temperature and pressure, potentially enabling product isolation and solvent purification in a single step. A free electron in solution makes an ideal probe of local solvent structure, and will help illuminate reactivity in these important media. Electrons with low energies are produced by field-enhanced photoemission from electrode surfaces in the solvent and the resulting current is detected with a second electrode. Experiments are being conducted at a new synchrotron facility at the Center for Advanced Microstructures and Devices in Baton Rouge, LA, and the resulting data are used to develop empirical models for the microscopic structure of the supercritical solvent systems.", "keywords": [], "approved": true } }, { "type": "Grant", "id": "1712", "attributes": { "award_id": "2029900", "title": "EAGER: Collaborative Research: Design of Inhibitors for ORF7a and ORF7b Oligomerization in COVID-19", "funder": { "id": 3, "ror": "https://ror.org/021nxhr62", "name": "National Science Foundation", "approved": true }, "funder_divisions": [ "Mathematical and Physical Sciences (MPS)" ], "program_reference_codes": [ "096Z", "7916" ], "program_officials": [ { "id": 4483, "first_name": "Catalina", "last_name": "Achim", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [] } ], "start_date": "2020-06-15", "end_date": "2022-05-31", "award_amount": 150000, "principal_investigator": { "id": 4484, "first_name": "Jeffery B", "last_name": "Klauda", "orcid": null, "emails": "[email protected]", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [ { "id": 297, "ror": "https://ror.org/047s2c258", "name": "University of Maryland, College Park", "address": "", "city": "", "state": "MD", "zip": "", "country": "United States", "approved": true } ] }, "other_investigators": [], "awardee_organization": { "id": 297, "ror": "https://ror.org/047s2c258", "name": "University of Maryland, College Park", "address": "", "city": "", "state": "MD", "zip": "", "country": "United States", "approved": true }, "abstract": "With this award, the Chemistry of Life Processes Program in the Chemistry Division and the Chemical and Biochemical Engineering Program in the Chemical, Bioengineering, Environmental and Transport Systems Division are funding Dr. Bryan Berger (University of Virginia) and Dr. Jeffery Klauda (University of Maryland) to investigate two proteins named ORF7a and OR7b from the COVID19 virus that have been implicated in how harmful the virus is to its host, e.g. the human cells. The research will focus on how these two proteins form larger protein complexes that in turn affect the interactions between the virus and the infected cells and influence the immune response of the host. The research informs the development of peptides that could be used to probe the viral propagation. The research is based on the use of a combination of computational and experimental methods. Dr. Berger and Dr. Klauda distribute to the scientific community free of charge through Addgene the plasmids and associated protocols developed for this project, thus enabling the global scientific community that works on finding a solution to the current pandemic and to minimizing the possibility of future outbreaks to quickly use the outcomes of their research. This work will provide training for post-doctoral fellows working on critical challenges using state-of-the-art experimental and computational methods. The results of the research will be disseminated by the team to the greater community through conferences and workshops at University of Virginia and University of Maryland and through publications. The researchers also plan to inform and educate students on possible mechanisms of virus transmission and prevention by participation in existing outreach programs at their Institutions.This research project seeks to understand the basis of specificity for transmembrane and juxtamembrane oligomerization of ORF7a with BST-2 and for homooligomerization of ORF7b. Using bacterial transcriptional assays for membrane protein dimerization based on the E. coli AraC protein (AraTM and DN-AraTM assays), the researches determine specific amino acid residues and structural motifs responsible for the protein oligomerization in bacterial membranes. This knowledge informs computational models for formation of BST-2/ORF7a heterooligomers and ORF7b homooligomers. In turn, the computational models are used to make critical new predictions of sequences for transmembrane peptides that could influence protein-protein interactions involving ORF7a and ORF7b. These predictions and the properties of the peptides are tested by synthesizing peptide libraries and using AraTM, DN-AraTM, and mammalian, cell-based fluorescence resonance energy transfer assays. Validation of candidate sequences are achieved using mammalian cell-based assays for BST-2 function and apoptosis. The results of these studies could provide high-resolution, experimentally validated models for OR7a and ORF7b homo and heterooligomerization, as well as peptide sequences that can be used to probe the roles of ORF7a and ORF7b in viral propagation in vivo.This grant is being awarded using funds made available by the Coronavirus Aid, Relief, and Economic Security (CARES) Act supplement allocated to MPS and ENG.This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.", "keywords": [], "approved": true } }, { "type": "Grant", "id": "1713", "attributes": { "award_id": "2029895", "title": "EAGER: Collaborative Research: Design of Inhibitors for ORF7a and ORF7b Oligomerization in COVID-19", "funder": { "id": 3, "ror": "https://ror.org/021nxhr62", "name": "National Science Foundation", "approved": true }, "funder_divisions": [ "Mathematical and Physical Sciences (MPS)" ], "program_reference_codes": [ "096Z", "7916" ], "program_officials": [ { "id": 4485, "first_name": "Catalina", "last_name": "Achim", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [] } ], "start_date": "2020-06-15", "end_date": "2022-05-31", "award_amount": 150000, "principal_investigator": { "id": 4486, "first_name": "Bryan W", "last_name": "Berger", "orcid": "https://orcid.org/0000-0002-6135-8677", "emails": "[email protected]", "private_emails": "", "keywords": null, "approved": true, "websites": "['http://www.addgene.org/']", "desired_collaboration": null, "comments": null, "affiliations": [ { "id": 517, "ror": "", "name": "University of Virginia Main Campus", "address": "", "city": "", "state": "VA", "zip": "", "country": "United States", "approved": true } ] }, "other_investigators": [], "awardee_organization": { "id": 517, "ror": "", "name": "University of Virginia Main Campus", "address": "", "city": "", "state": "VA", "zip": "", "country": "United States", "approved": true }, "abstract": "With this award, the Chemistry of Life Processes Program in the Chemistry Division and the Chemical and Biochemical Engineering Program in the Chemical, Bioengineering, Environmental and Transport Systems Division are funding Dr. Bryan Berger (University of Virginia) and Dr. Jeffery Klauda (University of Maryland) to investigate two proteins named ORF7a and OR7b from the COVID19 virus that have been implicated in how harmful the virus is to its host, e.g. the human cells. The research will focus on how these two proteins form larger protein complexes that in turn affect the interactions between the virus and the infected cells and influence the immune response of the host. The research informs the development of peptides that could be used to probe the viral propagation. The research is based on the use of a combination of computational and experimental methods. Dr. Berger and Dr. Klauda distribute to the scientific community free of charge through Addgene the plasmids and associated protocols developed for this project, thus enabling the global scientific community that works on finding a solution to the current pandemic and to minimizing the possibility of future outbreaks to quickly use the outcomes of their research. This work will provide training for post-doctoral fellows working on critical challenges using state-of-the-art experimental and computational methods. The results of the research will be disseminated by the team to the greater community through conferences and workshops at University of Virginia and University of Maryland and through publications. The researchers also plan to inform and educate students on possible mechanisms of virus transmission and prevention by participation in existing outreach programs at their Institutions.This research project seeks to understand the basis of specificity for transmembrane and juxtamembrane oligomerization of ORF7a with BST-2 and for homooligomerization of ORF7b. Using bacterial transcriptional assays for membrane protein dimerization based on the E. coli AraC protein (AraTM and DN-AraTM assays), the researches determine specific amino acid residues and structural motifs responsible for the protein oligomerization in bacterial membranes. This knowledge informs computational models for formation of BST-2/ORF7a heterooligomers and ORF7b homooligomers. In turn, the computational models are used to make critical new predictions of sequences for transmembrane peptides that could influence protein-protein interactions involving ORF7a and ORF7b. These predictions and the properties of the peptides are tested by synthesizing peptide libraries and using AraTM, DN-AraTM, and mammalian, cell-based fluorescence resonance energy transfer assays. Validation of candidate sequences are achieved using mammalian cell-based assays for BST-2 function and apoptosis. The results of these studies could provide high-resolution, experimentally validated models for OR7a and ORF7b homo and heterooligomerization, as well as peptide sequences that can be used to probe the roles of ORF7a and ORF7b in viral propagation in vivo.This grant is being awarded using funds made available by the Coronavirus Aid, Relief, and Economic Security (CARES) Act supplement allocated to MPS and ENG.This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.", "keywords": [], "approved": true } }, { "type": "Grant", "id": "2964", "attributes": { "award_id": "1905374", "title": "Mechanistic investigation of DNA cleavage and specificity in CRISPR-Cas9", "funder": { "id": 3, "ror": "https://ror.org/021nxhr62", "name": "National Science Foundation", "approved": true }, "funder_divisions": [ "Mathematical and Physical Sciences (MPS)", "Chemistry of Life Processes" ], "program_reference_codes": [], "program_officials": [ { "id": 9021, "first_name": "Catalina", "last_name": "Achim", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [] } ], "start_date": "2019-09-01", "end_date": "2022-08-31", "award_amount": 450000, "principal_investigator": { "id": 9022, "first_name": "Giulia", "last_name": "Palermo", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [ { "id": 153, "ror": "", "name": "University of California-Riverside", "address": "", "city": "", "state": "CA", "zip": "", "country": "United States", "approved": true } ] }, "other_investigators": [], "awardee_organization": { "id": 153, "ror": "", "name": "University of California-Riverside", "address": "", "city": "", "state": "CA", "zip": "", "country": "United States", "approved": true }, "abstract": "With this award, the Chemistry of Life Processes Program in the Chemistry Division is funding Dr. Giulia Palermo from the University of California, Riverside, to investigate the molecular basis of DNA cleavage and specificity in the CRISPR (clustered regularly interspaced short palindromic repeat)-Cas9 system through computational methods. The CRISPR-Cas9 technology is a method that makes precise modification of the genome of an organism (including that of humans) possible. The technology is based on the use of a nuclease, an enzyme capable of cutting the double stranded DNA, and an RNA molecule that is bound to the enzyme and guides the enzyme to the site in the DNA where the cut is to take place. This research seeks to understand the mechanism by which the enzyme functions using computational methods developed by Dr. Palermo and her collaborators. The results of this study may aid in the development of more efficient genome editing technologies and their applications in biological research, biofuels production, and the development of drought-resistant crops with enhanced nutritional value. The project involves an outreach and mentoring program, which includes hands-on sessions for high school students from underrepresented minority groups and teachers.\n\nCRISPR-Cas9 is a bacterial adaptive immune system that is revolutionizing basic and applied life sciences by enabling a facile genome editing technology. This project provides detailed understanding of how this system edits and manipulates nucleic acids, which is of importance for improving the genome editing capability. This research project seeks to characterize the mechanism of DNA cleavage and specificity of the Streptococcus Pyogenes (Sp) CRISPR-Cas9 system by using state-of-the-art computational methods. The project employs a mixed quantum mechanics/molecular mechanics (QM/MM) approach and ab-initio Molecular Dynamics (MD) simulations (using the Born-Oppenheimer and Car-Parrinello approaches) in combination with free energy methods to investigate the catalytic mechanism of DNA cleavage in CRISPR-Cas9. These methodologies may elucidate the catalytic role of metal ions, which are critical for the enzymatic processing of DNA. Classical MD and enhanced sampling techniques are employed to investigate the mechanism of DNA specificity, characterizing the conformational changes arising from the binding of altered DNA sequences and how they affect the catalysis. Theoretical investigations are performed in collaboration with experimentalists. The new theory assists in the interpretation of experimental data and makes possible predictions that can be tested in the laboratory.\n\nThis award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.", "keywords": [], "approved": true } }, { "type": "Grant", "id": "4174", "attributes": { "award_id": "1608009", "title": "CDS&E: Cyclic Tetrapeptide Probes For Protein Binding", "funder": { "id": 3, "ror": "https://ror.org/021nxhr62", "name": "National Science Foundation", "approved": true }, "funder_divisions": [ "Mathematical and Physical Sciences (MPS)", "Chemistry of Life Processes" ], "program_reference_codes": [], "program_officials": [ { "id": 14052, "first_name": "Max", "last_name": "Funk", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [] } ], "start_date": "2016-09-01", "end_date": "2020-08-31", "award_amount": 500000, "principal_investigator": { "id": 14054, "first_name": "Kevin", "last_name": "Burgess", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [ { "id": 342, "ror": "https://ror.org/01f5ytq51", "name": "Texas A&M University", "address": "", "city": "", "state": "TX", "zip": "", "country": "United States", "approved": true } ] }, "other_investigators": [ { "id": 14053, "first_name": "Thomas R", "last_name": "Ioerger", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [] } ], "awardee_organization": { "id": 342, "ror": "https://ror.org/01f5ytq51", "name": "Texas A&M University", "address": "", "city": "", "state": "TX", "zip": "", "country": "United States", "approved": true }, "abstract": "With this award, the Chemistry of Life Processes Program in the Chemistry Division is funding Dr. Kevin Burgess of Texas A & M University to discover small molecules that affect how some proteins bind to each other. Protein-protein interactions are important to many biological processes in cells. Thus having small molecules that can either aid or or hinder protein-protein interactions could lead to potential new drugs to help treat various diseases. The project is creating new small molecules and studying their effect on protein-protein interactions. It also combines chemical synthesis, computer-aided molecular design and data-mining training for graduate and undergraduate students to help them tackle problems in contemporary life science. \n\nCyclic peptides are known to mimic key regions involved in protein-protein interactions, i.e. to be Protein-Protein Interface (PPI) mimics. While cyclic pentapeptides are easy to make they tend to equilibrate between conformers. Conversely cyclic tetrapeptides from natural amino acids are difficult to make but are more conformationally stable. Thus, easily synthesized cyclic peptides from genetically encoded amino acids linked by main-chain amides can have ring sizes of 9, 12, 15, etc. i.e. 3n atoms, (n = # amino acids) which misses ring sizes between 12 and 15 that combine conformational rigidity with ease of synthesis. This work is showing that contrary to some earlier reports, cyclic Tetrapeptides from natural amino acids are conformationally rigid and are more synthetically accessible than previously thought. It is also showing that replacement of a genetically encoded residue with some rigid unnatural amino acids can be used to give cyclic tetrapeptides that rest at a useful crossroads between ease of synthesis and conformational rigidity.", "keywords": [], "approved": true } }, { "type": "Grant", "id": "1549", "attributes": { "award_id": "2037695", "title": "RAPID: Developing a universal modular platform to engineer coronavirus vaccine candidates", "funder": { "id": 3, "ror": "https://ror.org/021nxhr62", "name": "National Science Foundation", "approved": true }, "funder_divisions": [ "Mathematical and Physical Sciences (MPS)" ], "program_reference_codes": [ "096Z", "7914" ], "program_officials": [ { "id": 4041, "first_name": "Pui", "last_name": "Ho", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [] } ], "start_date": "2020-07-15", "end_date": "2022-06-30", "award_amount": 200000, "principal_investigator": { "id": 4042, "first_name": "Angad P", "last_name": "Mehta", "orcid": null, "emails": "[email protected]", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [ { "id": 281, "ror": "", "name": "University of Illinois at Urbana-Champaign", "address": "", "city": "", "state": "IL", "zip": "", "country": "United States", "approved": true } ] }, "other_investigators": [], "awardee_organization": { "id": 281, "ror": "", "name": "University of Illinois at Urbana-Champaign", "address": "", "city": "", "state": "IL", "zip": "", "country": "United States", "approved": true }, "abstract": "With this award, the Chemistry of Life Processes program in the Chemistry Division supports the studies by Dr. Angad Mehta at the University of Illinois at Urbana-Champaign to make live attenuated forms of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) that require an unnatural compound to reproduce. SARS-CoV-2 is the virus that causes coronavirus disease 2019 (COVID-19). Live-attenuated viruses have reduced abilities to cause disease, but remain capable of providing immunity in humans. As such, live-attenuated viruses represent one of the effective strategies for the development of vaccines against wide-spread viral infections. The genomic RNA of the virus must be modified with a methyl group in order to be copied by infected cells, and this methyl group is added by enzymes using the natural compound S-adenosylmethionine (AdoMet). Dr. Mehta’s project engineers SARS-CoV-2 particles that use synthetic forms of AdoMet (called xAdoMet) for this critical methylation step. The resulting engineered SARS-CoV-2* is a live virus in a laboratory, where xAdoMet can be added as a required supplement. The SARS-CoV-2*, however, cannot reproduce in normal cells, where xAdoMet is not present, but can still result in an immune response in an infected patient. The impact on society is that a unique platform is engineered for the development of vaccines to address viral diseases, including the COVID-19 pandemic. The broader impacts of this project include the strong cross-disciplinary training of graduate students.This goal of this study is to develop live attenuated SARS-CoV-2 particles that are dependent on an unnatural version of an essential cofactor for its replication that is added in a laboratory setting, but not available in the infected host. SARS-CoV-2 requires S-adenosylmethionine (AdoMet) as a cofactor for a critical methylation of the viral RNA by a methyl transferase in order to translate its genes and replicate its genome. Through this project, a strain of the coronavirus (SARS-CoV-2*) is engineered that utilizes and is dependent on an unnatural analogue of AdoMet (xAdoMet) for the critical methylation reactions. Such a virus requires supplements of xAdoMet in a laboratory in order to replicate. Once injected into a host, this viral strain can infect a cell and potentially induce an immune response in the host, but cannot replicate in the absence of exogenous supplementation with xAdoMet. The objectives are to synthesize a series of xAdoMet compounds; use the xAdoMet compounds to engineer SARS-CoV-2* through directed evolution; and test the live attenuated virus for induction of immune response in cell culture. The AdoMet-dependent methylation mechanism is conserved in all known coronavirus pathogens and, therefore, has the potential to serve as a far-reaching and modular platform for vaccine development well beyond SARS-CoV-2.This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.", "keywords": [], "approved": true } }, { "type": "Grant", "id": "14106", "attributes": { "award_id": "2147792", "title": "Plasmon-induced Triplet Energy Transfer (PITET) for Photon Upconversion", "funder": { "id": 3, "ror": "https://ror.org/021nxhr62", "name": "National Science Foundation", "approved": true }, "funder_divisions": [ "Mathematical and Physical Sciences (MPS)", "OFFICE OF MULTIDISCIPLINARY AC" ], "program_reference_codes": [], "program_officials": [ { "id": 30636, "first_name": "John", "last_name": "Papanikolas", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [] } ], "start_date": "2021-09-01", "end_date": null, "award_amount": 450000, "principal_investigator": { "id": 30637, "first_name": "Ming", "last_name": "Tang", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [] }, "other_investigators": [], "awardee_organization": { "id": 202, "ror": "https://ror.org/03r0ha626", "name": "University of Utah", "address": "", "city": "", "state": "UT", "zip": "", "country": "United States", "approved": true }, "abstract": "With this award, the Macromolecular, Supramolecular, and Nanochemistry Program in the Chemistry Division is supporting Dr. Ming Lee Tang at the University of California Riverside (UCR) to study the energy transfer process of plasmonic systems. Plasmonics refers to light-induced oscillation of loosely bound electrons in metals. This research is important for catalysis, imaging, and energy conversion applications. Minuscule metal particles with dimensions on the order of nanometers have been treasured historically for their beauty in stained glass windows. The vivid colors in stained glass arise from the strong absorption and scattering of light due to plasmons supported by the metal nanoparticles. Dr. Tang’s team is conducting fundamental research that addresses that seeks to efficiently transfer the energy stored as plasmons in metal nanoparticles to neighboring chemical molecules. The research aims to provide mechanisms to prevent the system from unwanted energy loss through rapid scattering of light or dissipation of energy as heat. Such advances are essential for the development of metal nanoparticles for intended applications in photocatalysis and in solar cells. The team designs and synthesizes various nanomaterial architectures. Plasmons tightly confined within the nanoscale metal architectures are then characterized to tune the system to perform useful work upon light activation. This research also has broader impacts of engaging the general public in the Inland Empire program in Southern California. This outreach program includes interactive demonstrations and science activities at local elementary schools and pre-schools that are led by undergraduate and graduate students.<br/><br/>Dr. Ming Lee Tang’s team at UCR is investigating plasmon-induced triplet energy transfer. The goal is to use light captured by metal nano-antennas for photon upconversion, a process of converting low energy photons from incoherent sources such as the sun to useful high energy photons. Novel light-absorbing nanostructures based on noble metals in this research can absorb near-infrared photons to produce violet photon emissions from neighboring anthracene- and perylene-based chromophores. Specifically, silver nanoprisms and gold nanorods with their localized surface plasmon resonance tuned between 1.5 and 1.8 eV are expected to be resonant with the lowest excited triplet states of the chromophores, so as to photosensitize the molecular triplet states across an oxide barrier. Steady-state photon upconversion measurements will be used to quantify the efficiency of plasmon-induced triplet energy transfer. Time resolved photoluminescence and transient absorption measurements provide independent measurements of the yield and rate of the triplet energy transfer.<br/><br/>This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.", "keywords": [], "approved": true } }, { "type": "Grant", "id": "5403", "attributes": { "award_id": "0640934", "title": "Fluorous Proteins: Structure, Stability, and Biological Activity", "funder": { "id": 3, "ror": "https://ror.org/021nxhr62", "name": "National Science Foundation", "approved": true }, "funder_divisions": [ "Unknown", "BIMOLECULAR PROCESSES" ], "program_reference_codes": [], "program_officials": [], "start_date": "2007-08-15", "end_date": "2010-07-31", "award_amount": 435000, "principal_investigator": { "id": 18901, "first_name": "E. Neil", "last_name": "Marsh", "orcid": null, "emails": "[email protected]", "private_emails": null, "keywords": "[]", "approved": true, "websites": "[]", "desired_collaboration": "", "comments": "", "affiliations": [ { "id": 169, "ror": "", "name": "Regents of the University of Michigan - Ann Arbor", "address": "", "city": "", "state": "MI", "zip": "", "country": "United States", "approved": true } ] }, "other_investigators": [ { "id": 18900, "first_name": "Hashim M", "last_name": "Al-Hashimi", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [] } ], "awardee_organization": { "id": 169, "ror": "", "name": "Regents of the University of Michigan - Ann Arbor", "address": "", "city": "", "state": "MI", "zip": "", "country": "United States", "approved": true }, "abstract": "With this award, the Organic and Macromolecular Chemistry Program supports Neil Marsh and Hashim M. Al-Hashimi both of the University of Michigan whose research will advance the area of protein design by engineering some of the novel properties of fluorocarbons into biological molecules. This will be achieved by synthesizing proteins that contain extensively fluorinated ('fluorous') analogs of hydrophobic amino acids in their hydrophobic cores. Fluorous amino acids are predicted to stabilize proteins against unfolding by heat and organic solvents and to facilitate protein: protein recognition through specific fluorocarbon-fluorocarbon interactions. Fluorinated versions of a dimeric RNA-binding protein, Rop, will be synthesized in which the hydrophobic core of Rop will be repacked with the fluorous analog of leucine, hexafluoroleucine. This protein is small enough (63 residues) to be efficiently synthesized by peptide synthesis, which will allow fluorous amino acids to be introduced site specifically. Rop protein has been extensively used as a model system for investigating protein stability and folding, and as a template for protein re-design. These data will serve as a useful reference for the present study. A variety of physical techniques (such as circular dichroism, microcalorimetry and analytical ultracentrifugation) will be used to investigate the effect of fluorination on the biological activity, structure and stability of fluorous Rop proteins. An important innovation will be the use of residual dipolar coupling (RDC) NMR measurements to perform detailed comparisons of the effect of fluorination on the structure and conformational rigidity of the protein. The experiments will address fundamental questions about the impact of fluorination on protein structure and dynamics.\nThis award from the Organic and Macromolecular Chemistry Program supports Professors Neil Marsh and Hashim M. Al-Hashimi both of the University of Michigan whose research will impact attempts to design biosensors and enzymes used in industrial processes, where stability towards extremes of temperature and pH and towards organic solvents is necessary. There is the potential for fluorous proteins to find uses in medical imaging by exploiting the high NMR sensitivity of Fluorine 19 or their enhanced biological stability could lead to uses as therapeutic agents or vehicles for drug delivery. The project will advance the education, training and professional development of undergraduates, graduate students and postdoctoral scientists in the inter-disciplinary area of chemical biology and biophysics. To broaden their education further, a joint interdisciplinary group meeting and journal club will be initiated. Their professional development will be enhanced by active participation in the dissemination of their results, both through drafting manuscripts and progress reports, and through oral and poster presentations at local and national scientific meetings.", "keywords": [], "approved": true } } ], "meta": { "pagination": { "page": 1393, "pages": 1405, "count": 14046 } } }