KU CREATORS Symposium

Program Info

Schedule

Keynote Speakers

Sambuddha Banerjee, Ph.D.

Speaker Bio: Sambuddha Banerjee, Ph. D. received their education from Calcutta, India before they moved to the US, initially for their postdoctoral research at Duke University, and then for his current position at ECU Chemistry. They identify as a gender non-conforming brown queer scientist-activist-philosopher and try to implement critical race and critical queer theories in their practice as a mentor. Their research interest includes investigating roles of transition metals in infection and immunity, use of small metal complexes as potential therapeutics, and analyzing scientific epistemology using critical race and queer theory. They are currently the Chair elect of the Minority Affairs Sub-division at the American Chemical Society and are also actively involved with several LGBTQIA2S+ inclusive antiracist STEM organizations.

Presentation title: Tracing the History of radical human rights movements & the STEM Academy

Presentation Abstract: The way it is important to know the genetic code of organisms to learn about their life, it is crucial we know the genetic code of resistance that has brought us to this point in time in the STEM academy. This will allow us to understand how the current status quo, however it seems inevitable, is not a product of a natural evolutionary process of human history. There has been, and there still is, a deliberate and consistent effort in the academy to keep the "outsiders" out, by creating rules that to an uncritical mind can seem eternal. In this 40 min, the speaker, a queer brown gender non-conforming feminist-scientist-philosopher will create a space to be brave, ask questions, and leave with more questions that need deep and intersectional approaches to answer.

Julian R. Silverman, Ph.D.

Alumni Panel Participants

• John Michael Handley
• Harrison Baker 
• Joshua Van Auken (online)
• Natacha Namphengsone (online)

Oral Presentation Abstracts

David Coria – Physics and Astronomy

Cosmic Close-Ups: The Past, Present, and Future of Direct Imaging in Exoplanets

The field of exoplanets and the exploration of distant worlds is ever evolving. The major tools and techniques for characterizing exoplanets (e.g., Radial Velocity and Transmission Spectroscopy) rely on indirect observations of their host stars. However, recent advancements in direct imaging and spectroscopy techniques have allowed us to study gas giant exoplanets in unprecedented detail. In this talk, I will highlight some of the early successes in direct imaging, then discuss recent studies using direct imaging and spectroscopy to derive exoplanet atmospheric abundances including my complementary work to characterize the volatile abundances in their host stars. By measuring carbon-to-oxygen and 12C/13C ratios in both the planet and host star, we may trace a planet's formation location and migration. I will also provide a glimpse into the science ushered in by next generation high-resolution spectrographs, adaptive optics, and coronagraphs on ground-based observatories like the ELT, GMT, TMT, space-based observatories like JWST and the HWO. Finally, I will discuss the challenges astronomers face as we push to extend direct imaging and spectroscopy to terrestrial exoplanets in the habitable-zone of sun-like stars.

Claire Cook – Physics & Astronomy

Where in the Galaxy Are We?

I am a post-bachelors astronomy researcher here at KU and I would like to give an engaging and accessible oral presentation, in drag, as my astronomy-themed drag king persona Astro Bites. The presentation would be for people of all astronomy knowledge levels and give an overview of the Milky Way galaxy and our place in it.

Erick McCloskey – Molecular Biosciences

Disruption of HSV-1 ICP0 Dimer Formation Impacts Important Protein Functions

Infected cell protein 0 (ICP0) is an important regulatory protein of herpes simplex virus 1 (HSV-1). ICP0 performs many of its functions, in part, through its C-terminal dimer domain (amino acids 555-767). Deletions in this dimer domain result in reduced viral gene expression, lytic infection, and reactivation from latency. Since ICP0’s dimer domain is associated with these important roles, we wanted to determine the structure of this specific domain and how the structure relates to these functions. ICP0 was purified from bacteria and analyzed by X-ray crystallography, revealing a composition of nine β-sheets and two α-helices. Interestingly, two adjacent β-sheets from one monomer “reach” into the adjacent subunit during dimer formation, generating two β-barrel-like motifs. Structural protein database searches indicate the fold/structure adopted by the ICP0 dimer is novel, and its dimer is held together by an extensive network of hydrogen bonds. This structure allowed for the identification of residues involved in dimer formation. These residues were substituted to alanine in order to create ICP0 dimer mutants incapable of dimer formation, while ideally preserving other functional domains in ICP0’s C-terminus. Preliminary data from promoter activation assays suggest dimer mutant ICP0 is unable to stimulate HSV-1 promoters as effectively as wild-type (WT) and is unable to fully complement the replication of an ICP0-null mutant. Additionally, dimer mutant virus shows reduced viral titer in mouse trigeminal ganglia (TG) compared to WT at day 5 following acute corneal infection. Intriguingly, dimer mutant protein stability appears to be increased compared to that of WT ICP0 during infection of HepaRG cells. Ongoing studies will continue to investigate the functions of ICP0 dimer formation and provide further insight into ICP0’s many activities and its role during HSV-1 infection.

Eliza K. Hanson – Chemistry

Individual recombinant repeats of MUC16 display variable binding to CA125 antibodies

Survival rates for ovarian cancer are dramatically improved if diagnosed at an early stage, but the majority of cases are not diagnosed until a later stage. CA125, a binding epitope on the large mucin protein MUC16, is an FDA-approved biomarker to monitor the recurrence of ovarian cancer but is not approved for diagnostic screening. The epitope is located within a region of many tandem repeats with similar amino acid sequences, but the exact location of the epitope has long been an important gap in our knowledge. A complete characterization of the tandem repeat domain will yield important insight into why CA125 may be under detected in some patients and offer the chance to critically develop new affinity reagents that can improve the detection and therefore the utility of this biomarker. The antibodies used in the clinical test (OC125 and M11) have shown variable binding when used to probe individually expressed recombinant tandem repeat proteins. To determine the location of the CA125 epitope, we performed the most comprehensive study to date studying the binding of individual recombinant tandem repeat proteins with clinically relevant antibodies. We expressed the tandem repeat proteins in E. coli and measured binding affinity via Western blot, ELISA, and SPR assays. We observed variable binding to the tandem repeats from different antibodies and across different analytical methods. The Western blot assays, which involve denaturing the repeats, demonstrated different patterns of binding than the ELISA and SPR carried out on protein in their native states, suggesting that some of the repeats may have a conformational epitope that is disrupted by denaturation. In addition, the differences in repeat recognition by antibodies in the same epitope groups indicate that these antibodies may not bind in the same location as was concluded based on initial competition assays. 

Samuel Brunclik – Chemistry

Investigation of ligand sphere perturbations on MnIII-alkylperoxo complexes

Drawing inspiration from manganese dependent enzymes, a range of synthetic manganese catalysts have been developed to carry out a variety of highly stereo-selective oxidation reactions such as olefin epoxidations. In these synthetic catalysts, a key step in the proposed catalytic mechanism invokes the heterolysis of the oxygen-oxygen bond of a MnIII-hydroperoxo intermediate to generate the active oxidant - a manganese(V)-oxo species. However, the geometric and electronic factors controlling this critical O-O activation step remain poorly understood. Work by our group and others has utilized MnIII-alkylperoxo complexes to mimic the key MnIII-hydroperoxo intermediates. From these investigations, there has been evidence that MnIII-alkylperoxo complexes can decay by both O-O homolysis and heterolysis pathways. Presumably, perturbations in the ligand-sphere of these MnIII-alkylperoxo complexes, specifically at positions trans to the O-O bond, could be employed to modulate the decay process. To that end, a new MnIII-alkylperoxo complex has been developed to investigate the effect of trans perturbations on the mechanism of cleavage of the oxygen-oxygen bond. A series of combined computational and kinetic investigations was completed with the goal of probing the effects of such a change to the ligand-sphere on the decay mechanism. These studies have allowed us to gain further understanding of the control of the ligand sphere over the reactivity of MnIII-alkylperoxo adducts.

Shuai Sun – Chemistry

Embedding DEI in General Chemistry: Insights from OER Book "Breaking Barriers: Diversity and Equity in Chemistry"

"Breaking Barriers: Diversity and Equity in Chemistry" is an open-access book that presents an innovative approach to integrating Diversity, Equity, and Inclusion (DEI) principles into General Chemistry education through Open Educational Resources (OER). This initiative leverages renewable assignments to foster a collaborative learning environment where students and faculty co-create dynamic, inclusive course materials. By engaging students in the development of content that highlights the contributions of underrepresented groups in science, the project aims to broaden perspectives within the scientific community and challenge prevailing stereotypes.

This presentation will outline the methodology behind the creation of "Breaking Barriers," emphasizing the participatory model of education that underpins the project. It will highlight the importance of embedding DEI in STEM curricula and the role of renewable assignments in achieving this goal. The collaboration with libraries in supporting and disseminating OER will be discussed, showcasing the critical role these institutions play in enhancing accessibility and equity in education.

Initial outcomes of the project, including shifts in student perceptions and attitudes towards DEI in the sciences, will be shared. The presentation will also explore the broader implications of this work for STEM education and the potential for OER to serve as a catalyst for change in creating a more inclusive and equitable academic and professional landscape in the sciences.

"Breaking Barriers" not only exemplifies the transformative power of OER in addressing educational disparities but also serves as a model for future endeavors aimed at fostering diversity and inclusion in higher education. This project highlights the synergy between collaborative content creation and the promotion of DEI principles, illustrating a path forward for integrating these essential values into the fabric of STEM education.
 

Sponsors

Gold ($2,000+)
Silver ($1,000–$1,999): Associate Dean for CLAS Maria Orive, Chemistry, Graduate Studies, K-INBRE, Geology, KU Office of Research
Bronze ($500–$999): Center for Environmentally Beneficial Catalysis, Ecology and Evolutionary Biology
 

Register to attend

Submit a poster presentation abstract

Download our flyer (PDF)