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Better Futures for Iowans Grants

Through the FUTURE in Biomedicine℠ program, the University of Iowa Carver College of Medicine is committed to:

  • Fostering closer research collaborations between its faculty and those of primarily undergraduate institutions throughout the state of Iowa.
  • Mentoring talented undergraduates who will be our next generation of physicians and biomedical scientists.
  • Promoting opportunities to translate biomedical discoveries and methods into educational materials used in Iowa's college classrooms.
  • Making its research facilities available to a statewide network of scientist-educators.

Consistent with these commitments, the goal of the Better Futures for Iowans program is to make state-of-the-art core research facilities at the University of Iowa available to academic classes and research projects conducted primarily by undergraduates at 2-year and 4-year institutions in Iowa.

Faculty throughout the state are eligible to apply for small grants to support laboratory-intensive projects involving undergraduate students in "hands-on" inquiry.  Students take responsibility for the preparation of samples and analysis of data obtained.  All participants are invited to present a poster about their work at the FUTURE in Biomedicine℠ Research Symposium.  This activity, which was initiated with support from the Office of the Provost in 2013, extends University resources to Iowans and addresses an important goal of the University Strategic Plan - to provide better futures for Iowans.

Applications for the 2016-2017 Better Futures for Iowans Grants are now being accepted.  For best consideration, please submit applications by November 11, 2016.  The awards will be made as University of Iowa accounts for projects to be completed at a single UI core by June 30, 2017.

2016-2017 Grant Recipients

Shaun Bowman, PhD
Assistant Professor of Biology 
Laura Hecker, PhD
Assistant Professor of Biology
Identification of proteins associated with HEF-1 in human ocular cells following prostaglandin analog treatment
Adina Kilpatrick, PhD
Assistant Professor of Physics
Probing the Conformational Dynamics of a calmodulin-binding site on the skeletal muscle ryanodine receptor
Bonnie Hall, PhD
Associate Professor of Chemistry
Molecular Basis of Chemotherapeutic Treatments for Chronic Myeloid Leukemia
Michael LaGier, PhD
Assistant Professor of Biology  
Discovery of New Antibiotics Via the Small World Initiative
Byron Noordewier, PhD
Professor of Biology
Discovery Science: Bacteriophage Hunting in Microbiology
Derek Lyons, PhD
Assistant Professor of Chemistry
Lord of the Rings: Improving the hydrophilicity of alpha-helix mimetics
Kelly Grussendorf, PhD
Assistant Professor of Natural and Applied Sciences
Use of model organism, Caenorhabditis elegans, to study the genetics and molecular mechanisms of muscular dystrophy
Douglas Brusich, PhD
Visiting Assistant Professor of Biology
Generation of phosphomutant fascin by CRISPR/Cas9 to study traumatic brain injury and nuclear regulation of actin


Clarke College - Shaun Bowman, PhD and Laura Hecker, PhD

"Glaucoma is a major cause of blindness in the United States, affecting more than 2 million Americans. The most important risk-factor for the development of glaucoma is elevated intraocular pressure (IOP). Therapeutic agents used in the management of elevated IOP include prostaglandin analogs (PAs) such as latanoprost-free acid (LFA), bimatoprost-free acid (BFA), and prostaglandin F2 alpha (PGF2α).  However, treatment with these PAs can result in unwanted side effects and the mechanism by which they lower IOP is unknown. Preliminary studies from our laboratory have shown that the human enhancer of filamentation 1 (HEF-1) protein expression is regulated by PAs in ocular cells. The collective actions of HEF-1 and its associated proteins are thought to modulate focal adhesion dynamics and function.  Increased expression of HEF-1 has been linked to increased cell migration and changes in cell growth and survival. It is currently unknown whether HEF-1 also functions in the regulation of IOP. Our preliminary results demonstrate that HEF-1 protein expression is increased in human ocular cells at 5 hours following treatment with PAs, LFA, BFA, and PGF2α. In addition, we have observed three proteins that have co-immunoprecipited with HEF-1 from PA treated cells. These putative binding partners will be identified by mass spectrometry. To do so, a senior biology major at Clarke University, Ryan Ryba, will perform the following: 1. Primary ocular cells will be cultured and treated with PAs for 5 hours 2. HEF-1 protein will be purified from monolayer cells using a commercially available antibody and an immunoprecipitation kit 3. Gel bands will be excised and submitted to the University of Iowa Proteomics Core Facility for identification."


Drake University - Adina Kilpatrick, PhD

"In skeletal muscle, the calcium binding protein calmodulin (CaM) plays an essential role in excitation-contraction coupling by modulating the opening and closing of the ryanodine receptor (RyR1), the main ion channel responsible for calcium release from the sarcoplasmic reticulum. Biochemical studies have mapped the CaM binding site (CaMBD) to a short region on RyR1 comprising residues 3614-3640. By interacting with this region differently at high and low calcium, CaM acts as a ‘switch’, providing essential feedback in calcium levels during muscle contraction. We are investigating structural and thermodynamic aspects of the CaM-RyR1 CaMBD interaction using a combination of fluorescence and NMR spectroscopy. In previous work, the thermodynamics of molecular recognition between CaM and RyR1 CaMBD was investigated using Förster resonance energy transfer (FRET) experiments in auto-fluorescent biosensor constructs. To complement the energetics studies, we are pursuing solution NMR studies of CaM/RyR1 peptide complexes. Co-expression of isotopically-labeled CaM-RyR1 CaMBD complexes at high calcium levels has enabled us for the first time to acquire 3D NMR data for the assignment of the backbone resonances of RyR1 CaMBD. In this project, we propose to acquire experiments for the determination of NMR relaxation parameters (15N T1, 15N T2, and {1H}-15N heteronuclear NOEs) of the RyR1 CaMBD backbone amide groups. These relaxation parameters will enable us to quantify the backbone conformational dynamics of CaM-bound RyR1 site. Undergraduate students will be involved in the analysis and interpretation of all NMR data."


Grand View University - Bonnie Hall, PhD

"CHEM 453, Biochemical Techniques, is a semester-long research-inspired undergraduate course offered at Grand View University.  Students examine the causes and consequences of the disruption of the Abl gene in Chronic Myeloid Leukemia (CML) patients (Taylor et al, 2010, Biochemistry and Molecular Biology Education 38:247-252).  Students study the effectiveness of first and second generation Tyrosine kinase inhibitors used for treating CML patients, and tie this information to molecular events occurring in the cancer cells.  One component of the course requires students to use primary literature to identify a specific mutation that confers resistance to first generation anti-CML agents, and to do site-directed mutagenesis to generate mutant protein for use in activity assays.  The students go on to examine the consequences of that mutation on responses to first and second generation therapeutic agents, working to understand that data within the context of the crystal structure of the ABL protein.  I am requesting funds for CHEM 453 students to use the Genomics Division IIHG facility.  Each student will perform a site-directed mutagenesis, and generate DNA samples, which will be sent to the Genomics division for sequencing.  The students will then analyze the sequence data to determine if each desired mutant was successfully generated.  Each will subsequently characterize the specific mutant generated, using biochemical and kinetic assays, and again tie that information to the molecular events known to occur in CML.  This will culminate in a formal written lab report, in the format of a journal article."


 Grand View University - Michael LaGier, PhD

"The Small World Initiative is global crowdsourcing effort to discover new antibiotics from soil bacteria; as one way to deal with the significant issue of antibiotic resistance among pathogens.  Grand View University undergraduate researchers will contribute to this project by sampling Iowa soils for the presence of new antibiotic-producing bacteria.  A key part of this project is the identification of identified antibiotic-producers by DNA sequencing, specifically 16s ribosomal RNA fingerprinting.  Funds supported by BBFI will provide the capital resources needed to carry out the RNA fingerprinting part of the SWI project."


Northwestern College - Byron Noordewier, PhD

"Over the past decade, the Northwestern College biology department has worked to embed discovery science into our course laboratories.  Our most recent endeavor in the area of discovery science as a pedagogical tool involves participation in a HHMI project called SEA-PHAGES (Scientific Education Initiative – Phage Hunters Advancing Genomic and Evolutionary Science).  Currently we are the only college in Iowa to participate the initiative which is divided into two portions:  a discovery phase and a bioinformatics phase.

In the discovery phase, each student will isolate a bacteriophage from their environmental soil samples.   Following isolation, the students are required to purify their bacteriophage and then characterize it including the preparation of a TEM grid for visualization via the project’s protocol and materials supplied by Northwestern College.  We anticipate bringing all of the samples from a class (about 24) to the University on a designated day along with some of the students so that they can observe as your technicians use TEM to visualize the students’ bacteriophages.  While the protocol for preparation is well established, we are open to any specific requirements which your facility deems important for successful microscopy.

HHMI provides protocols, technical assistance and project direction but the funding of on campus work is the responsibility of each participating institution.  We are requesting time and technical assistance from the University of Iowa core microscopy facility for our students to visualize their phages by TEM and for the Better Future for Iowans grant to provide a portion of the financial commitment."


Simpson College - Derek Lyons, PhD

"Modulation of cellular processes using small molecules continues to be a foundational methodology for advancing our understanding and treatment of diseases. Inhibition of protein-protein interactions is challenging because the protein interactions are often mediated by large, flat, hydrophobic surfaces. Andrew Hamilton’s laboratory at Yale University pioneered the use of the terphenyl structural moiety as a scaffold that mimics an alpha-helix structure. Specifically, the terphenyl scaffold mimics one face of an alpha-helix by positioning variable chemical moieties in the i, i+3, and i+7 locations. The first test of the effectiveness of the terphenyl scaffold in blocking a protein-protein interaction was performed by Hamilton’s laboratory, inhibiting the interaction between Calmodulin and Myosin Light-Chain Kinase (MLCK). Calmodulin is a protein whose structure is modulated by calcium concentrations within the cell. In turn, Calmodulin binds to and regulates the activity of other proteins, making calmodulin a mandatory participant in many cellular pathways. The terphenyl scaffold showed only a 10-fold higher IC50 than a 20-mer peptide of the native MLCK tail in an in vitro kinase activity assay, despite being significantly smaller than the native 20-mer peptide. 

Unfortunately, the phenyl rings of terphenyl scaffold make the structure extremely hydrophobic and only moderately soluble in aqueous solution, even in the presence of high percentages of DMSO. Hyun-Suk Lim’s laboratory, at Indiana University and Pohang University in South Korea, improved the hydrophilicity of the terphenyl scaffold by developing a triazine-piperazine-triazine scaffold. This scaffold has been shown to successfully inhibit alpha-helix mediated protein-protein interactions like MCL-1 and alpha-synuclein. 

We synthesized the triazine-piperazine-triazine mimetic of MLCK in an effort to compare Calmodulin inhibition of the triazine-piperazine-triazine scaffold with the previous generation terphenyl scaffold. Conformation of the structure of this large molecule has been attempted with GC-MS analysis and 60MHz NMR. Data from both techniques support the expected structure, but neither technique has proven adequate to confirm the structure. I am proposing to utilize the NMR core facilities at the University of Iowa to characterize the structure of both a MLCK mimetic and a control molecule that is a bare scaffold." 


University of Dubuque - Kelly Grussendorf, PhD

"With students at the University of Dubuque, we work to address molecular mechanisms of cellular and structural maintenance. Many of the cells and tissues that we are born with function throughout our entire lifetime! When there is development of mutations or disruptions in the maintenance of these structures, it often results in disease. 

We use the model organism, Caenorhabditis elegans, to address these questions. C. elegans serve as an ideal organism because of their many genetic capabilities, invariant cell lineage and transparency. Because of the transparency we are able to observe cellular and tissue structures live, throughout the lifetime of the organism. This also allows for us to observe any disruptions in these cellular and structural processes. Along with the transparency of the organism and molecular markers, such as Green Fluorescent Protein and other fluorescent markers, the ability to address these questions in C. elegans becomes ideal. 

We work to study muscular dystrophy, which is a disorder that develops when there is a loss in the structural maintenance of the muscular and nervous tissue. With the combination of characteristics of C. elegans, and ability to study genetics and molecular biology in this organism, we focus a lot of our work on microscopy and imaging. By use of different microscopic imaging we can address our questions and this gives the students the opportunity to carry out their own work, contribute to the scientific field, and advance their knowledge and skills in research which will support them in their future careers."


Wartburg College - Douglas Brusich, PhD

"Traumatic brain injury (TBI) is a common occurrence in the United States with over 2 million cases resulting in a hospital visit or death each year[1]. Aside from acute symptoms and risk of death proximal to injury, TBI is also associated with neurodegeneration[1–4]. However, the cellular mechanisms by which TBI predisposes animals to neurodegeneration remain unclear.

One group of pathways that is known to be activated downstream of TBI are cellular stress pathways[5,6]. Accumulation of nuclear actin is a known stress response pathway which is active under a range of stimuli including aging and neurodegeneration[7–9]. Preliminary research done in the lab of Dr. Tina Tootle, and supported by the FUTURE program, showed that fruit flies are a useful model to study cellular responses to TBI and that actin accumulates in the nucleus following TBI (unpublished data). This data suggests that regulation of nuclear actin is a cellular stress response activated downstream of TBI.

In separate research, the Tootle lab demonstrated that one key factor necessary for the nuclear regulation of actin is fascin[10]. Fascin is a highly conserved protein known for a canonical role in actin bundling. Fascin is regulated in part by phosphorylation at two highly conserved serine resides analogous to S52 and S289 in fruit flies[11,12]. Attempts to identify a role for fascin in outcomes following TBI were inconclusive, likely due in part to variations in genetic background. Genetic background is a key determinant of outcomes following TBI in fruit flies as evidenced by dramatically different sensitivities of several “wild-type” stocks when subjected to TBI[13]. However, advances in the use of the CRISPR/Cas9 system have resulted in cost-effective methods for doing gene editing in fruit flies that allow for control of genetic background[14,15]. 

I propose using the CRISPR/Cas9 system to generate phosphomutant fascin at both S52 and S289 residues in order to better study the role of fascin in nuclear regulation of actin following TBI. F0 fly embryos will be injected by students at Wartburg College and likely mutants will be selected in subsequent F1 progeny based on phenotypes known to be caused by loss of fascin, including bristle deformities and reduction of female fertility. DNA from likely mutants will be prepped by Wartburg College students and sent to the University of Iowa Genomics Division for DNA sequencing to confirm the desired genome edit at the appropriate fascin locus.

Importantly, the proposed project promises both educational and scholarly benefits. First, the use of the CRISPR/Cas9 technique will take place in the spring 2017 semester in the classroom laboratory as part of a Cellular and Molecular Neuroscience class I will teach. Thus, undergraduate students will be allowed hands-on practice in the most current techniques for genome editing in an instructional setting. Additionally, the generation of phosphomutant fascin will be used by my lab at Wartburg College to better determine a role for fascin and its regulation of actin downstream of TBI. My studies will build on an ongoing collaboration with the Tootle lab in which mechanisms of nuclear actin regulation uncovered in the germline by the Tootle lab are assessed for roles in responding to TBI in my own lab. Last, the Tootle lab has interest in using phosphomutant fascin for ongoing studies in the germline so successful generation of phosphomutant fascin promises to directly benefit research done at the University of Iowa."

1. CDC: Centers for Disease Control. No Title. Injury Prevention & Control: Traumatic Brain Injury & Concussion (2016). Available at: http://www.cdc.gov/traumaticbraininjury/get_the_facts.html. (Accessed: 9th May 2016)

2. Perry, D. C. et al. Association of traumatic brain injury with subsequent neurological and psychiatric disease: a meta-analysis. J. Neurosurg. 124, 511–26 (2016).

3. Daneshvar, D. H., Goldstein, L. E., Kiernan, P. T., Stein, T. D. & McKee, A. C. Post-traumatic neurodegeneration and chronic traumatic encephalopathy. Mol. Cell. Neurosci. 66, 81–90 (2015).

4. Young, J. S., Hobbs, J. G. & Bailes, J. E. The Impact of Traumatic Brain Injury on the Aging Brain. Curr. Psychiatry Rep. 18, 81 (2016).

5. Yu, W. et al. Oxidation of KCNB1 Potassium Channels Causes Neurotoxicity and Cognitive Impairment in a Mouse Model of Traumatic Brain Injury. J. Neurosci. 36, 11084–11096 (2016).

6. Stoica, B. A. & Faden, A. I. Cell Death Mechanisms and Modulation in Traumatic Brain Injury.

7. Maloney, M. T. & Bamburg, J. R. Cofilin-mediated neurodegeneration in Alzheimer’s disease and other amyloidopathies. Mol. Neurobiol. 35, 21–44 (2007).

8. Minamide, L. S., Striegl, A. M., Boyle, J. A., Meberg, P. J. & Bamburg, J. R. Neurodegenerative stimuli induce persistent ADF/cofilin-actin rods that disrupt distal neurite function. Nat. Cell Biol. 2, 628–36 (2000).

9. Munsie, L. et al. Mutant huntingtin causes defective actin remodeling during stress: defining a new role for transglutaminase 2 in neurodegenerative disease. Hum. Mol. Genet. 20, 1937–51 (2011).

10. Kelpsch, D. J., Groen, C. M., Fagan, T. N., Sudhir, S. & Tootle, T. L. Fascin regulates nuclear actin during Drosophila oogenesis. Mol. Biol. Cell 27, 2965–2979 (2016).

11. Sedeh, R. S. et al. Structure, evolutionary conservation, and conformational dynamics of Homo sapiens fascin-1, an F-actin crosslinking protein. J. Mol. Biol. 400, 589–604 (2010).

12. Zanet, J. et al. Fascin promotes filopodia formation independent of its role in actin bundling. J. Cell Biol. 197, 477–486 (2012).

13. Katzenberger, R. J. et al. A Drosophila model of closed head traumatic brain injury. Proc. Natl. Acad. Sci. U. S. A. 110, E4152-9 (2013).

14. Gratz, S. J. et al. Genome engineering of Drosophila with the CRISPR RNA-guided Cas9 nuclease. Genetics 194, 1029–35 (2013).

15. Gratz, S. J., Harrison, M. M., Wildonger, J. & O’Connor-Giles, K. M. Precise Genome Editing of Drosophila with CRISPR RNA-Guided Cas9. Methods Mol. Biol. 1311, 335–48 (2015).