Rhea Bachani

Mentor: Brian Bachmann
Home Institution: Stevens Institute of Technology 

"Photometabolomics: A Comparative Activity Platform for the Discovery of Novel Polyene Macrolactams"

Polyene macrolactams (PMs) are an underinvestigated class of light-sensitive natural products known to exhibit potent and selective anticancer and antimicrobial activities. Our lab previously discovered ciromicins A and B, which are PM photoisomers that show differing cell-type selective activity in acute myeloid leukemia patient samples. The selective activity of other PMs and their photoisomers remains largely unexplored, and microbial genome analysesrevealed many undiscovered novel PMs. To further explore PMs and characterize activity, we employed a photometabolomics workflow combiningcomparative and activity metabolomics, where crude extracts maintained in light-shielded conditions are divided and either exposed to broad spectrum UV/Vis light or kept in darkness. Comparative metabolomics identified altered metabolites following light exposure, performed using Ultra High Performance Liquid Chromatography-Mass Spectrometry (UHPLC-MS), with metabolomic features compared using multivariate statistical analysis. In parallel, we createdmetabolomic array assay plates through split-flow HPLC-MS such that each well corresponds to one minute of UV/MS data. Light and low-light conditioned extracts were tested for activity in bacteria and human cells lines, and bioactive wells were correlated to specific mass features using Multiplexed ActivityMetabolomics (MAM). We identified mass features that change in intensity, retention time, and/or activity between low-light and UV/Vis exposed conditions. Notably, the Kutzneria viridogrisea extract demonstrates growth inhibition of Staphylococcus aureus in 8 wells in the light condition that are absent in the light-shielded condition, and also shows activity against MV4-11 human leukemia cell lines across several concentrations. These results suggest that Kutzneria viridogrisea produces natural products with light-dependent antibacterial activity and anticancer activity, warranting isolation, structure elucidation, and characterization of the antibacterial compound for further development.

Bio. Rhea Bachani is a rising senior at Stevens Institute of Technology studying chemical biology. At Stevens, her research focuses on utilizing and experimentally validating an AI-driven workflow to develop inhibitors for Mixed Lineage Kinase 4, which is implicated in triple negative breast cancer. She served as the Vice President of the Stevens Chapter of ACS and earned the ACS New York Section Excellence in Chemical Sciences Award. After graduation, she plans to pursue a PhD in biochemistry.

Rhea Bachani

Mentor: Jeffrey N. Johnston
Home Institution: Elon University

"Synthesis of Residues A and D for the Total Synthesis of the Natural Product Complestatin"

Complestatin is a structurally complex peptide natural product with side chain cross-links that create macrocyclic conformational constraints. It is an antibioticwith demonstrated HIV-inhibitory activity. This project aimed to develop an efficient synthetic route toward residues A and D of complestatin. The enantioselective synthesis of nitroalkene-derived intermediates uses an organocatalytic Amidine-Amide (AmA) catalyzed reduction to provide enantioenriched substrates for Umpolung Amide Synthesis (UmAS). The proposed route involved the preparation of residues A and D throughenantioselective nitroalkene transformations, reduction reactions, protecting-group manipulations, and UmAS-based peptide bond formation. Residue A wassuccessfully prepared and scaled up, and progress was made toward the synthesis and scale-up of residue D. Quantities of key intermediates were produced to supply subsequent efforts to prepare dipeptide and tripeptide fragments. These results are an early step toward improved access to key complestatin residues that ultimately enable the proposed synthesis, one that is expected to stimulate the study of complestatin’s biological activity and potential use as a therapeutic.

Bio. Rachel Brown is originally from Hollis, New Hampshire and is currently pursuing a Bachelor of Science in Chemistry at Elon University. Currently, Rachel is the Vice President of the American Chemical Society club at Elon University. She is currently engaged in research synthesizing and characterizing cobalt centered organometallic compounds as a part of the Elon College Fellows Program. Outside of Elon, Rachel participated in the University of Michigan College of Pharmacy REU where she gained experience in medicinal chemistry research working in small molecule drug discovery and optimization. This summer, Rachel has been researching the total synthesis of complestatin in the Johnston lab as a part of the Vanderbilt Chemical Biology NSF-REU 2026. Rachel is excited to return to Elon in the fall for her senior year and continue work as a General Chemistry recitation leader and Organic Chemistry Laboratory Teaching Assistant.

Jazmine Buxton

Mentor: Lars Plate
Home Institution: Berry College 

"Cellular Thermal Shift Assay (CETSA) to characterize CFTR stability in response to correctors"

Cystic fibrosis (CF) is a lethal genetic disorder caused by mutations in the Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) chloride channel that can impair its folding, trafficking, or gating. L165S is a rare misfolding mutation that has received little attention in the literature, making it an important target for our investigation. Cell surface biotinylation assays show that VX-445+VX-661 corrector drug treatment rescues L165S-CFTR cell surface expression to half of wild-type (WT), while a newer corrector, IDOR-4, rescues to near WT cell surface expression. However, Western blot analysis revealed similar amounts of mature CFTR (C-band, post-Golgi) in VX-445+VX-661, WT, and IDOR-4 treated cells. Previous CF studies have assumed that C-band abundance directly reflects the amount of CFTR present at the cell surface; these findings demonstrate that C-band is an imperfect proxy for cell-surface CFTR. Here we developed a Cellular Thermal Shift Assay (CETSA) for CFTR to directly measure the protein stability of L165S-CFTR in HEK293T cells under VX-445+VX-661 and IDOR-4 treatment with WT-CFTR conditions used as a reference stability. We hypothesized that VX-445+VX-661 shows a more limited effect in stabilizing L165S-CFTR and leads to less cell surface expression. CETSA and Western blot analysis showed that VX-445+VX-661 treated cells retained less L165S-CFTR at higher melting temperatures than either IDOR-4 treated or WT cells, both of which exhibited similar thermal stability. Thesefindings suggest that VX-445+VX-661 treatment incompletely stabilizes L165S-CFTR preventing adequate rescue of the protein. Overall, our study demonstrates that CETSA is a useful assay for evaluating drug-induced changes to CFTR stability in variant cell lines and purified protein. CETSA may improve our understanding of post-golgi CFTR regulation and provide insight into the L165S mutation, which is essential, as research on rare CF mutations can both support patients and reveal drug strategies relevant to other understudied variants.

Bio.  Jazmine Buxton is a senior Biochemistry major at Berry College and a participant in the Chemical Biology REU at Vanderbilt University. Her current research in the Plate Lab investigates the molecular basis of a rare cystic fibrosis mutation to help guide the development of future therapeutic strategies. Her previous research focused on equine diseases and the molecular interactions of COVID-19. She is passionate about uncovering the mechanisms behind genetic and infectious diseases as she plans to pursue a PhD in biomedical sciences. She also values mentorship, serving as a Peer Consultant for students on academic probation and as the Student Director of Marketing and Events for Berry College’s tutoring center.

Naima Charles

Mentor: Lars Plate
Home Institution: Davidson College 

"Effects of Synonymous Codon Mutations on Ubiquitination of the Foot-and-Mouth Disease P1 Polyprotein"

RNA viruses have evolved mechanisms to exploit host resources and rapidly mutate, making them a challenge to control. To overcome this, one strategy is the incorporation of synonymous mutations into viral genomes to weaken viruses for the development of live attenuated vaccines. Although synonymous mutations do not alter the amino acid sequence of a protein, they have been shown to reduce viral fitness while triggering the host immune response. In this study, we use foot-and-mouth disease virus (FMDV), a highly contagious livestock pathogen, as a model to investigate the effects of codon deoptimization ofthe FMDV P1 capsid precursor protein on interactions with the host protein homeostasis (proteostasis) network. Previous quantitative proteomics suggestedthat deoptimized P1 may be modified more extensively by ubiquitin than wild-type P1. Our research goal is to assess how codon deoptimization affects P1degradation. Here, wild-type P1 and deoptimized P1 were affinity purified, and both were treated with a deubiquitinase enzyme to quantify ubiquitinationlevels in the two proteins. We also examined K48 and K63 ubiquitin linkages to distinguish between proteasomal degradation and alternative cellular signaling. These findings could provide insight into the consequences of synonymous mutations on viral capsid degradation with implications for the development ofsafer and more effective live attenuated vaccines for RNA viruses.

Bio. Naima Charles is a senior at Davidson College majoring in Biology and minoring in Public Health. Her prior research experience includes quantifying parental behaviors in two different species of songbirds (zebra finches and society finches) to better understand human social development. Outside of the lab, she is the President of Girls in STEM, which focuses on reducing the gender gap in fields of science. After graduation, she plans to pursue clinical translational research.

Isabella Dennison

Mentor: F. Peter Guengerich
Home Institution: Grove City College

"Cytochrome P450 2J2 and FABp3; A Potential Mechanistic Link to Cardiotoxicity"

Drug-induced cardiotoxicity is a complex interaction of different pharmacological agents causing a cascade of chemical reactions, leading to changes inelectrocardiographic (ECG) waveform morphology, hemodynamics, pathologic damage to the myocardium and vasculature, and changes in blood function. Drug-induced cardiotoxicity impacts individuals who have been taking chemotherapy or other cancer drugs and often can result in conditions as severe as cardiac arrest. Cytochrome P450 (P450) is a family of heme-containing enzymes involved in numerous biosynthetic and metabolic pathways. P450 2J2, anenzyme located in cardiomyocytes, is responsible for oxidizing arachidonic acid to epoxyeicosatrienoic acids (EETs), which can be important in various critical regulatory pathways. Once drugs have been metabolized, arachidonic acid buildup can potentially lead to the cardiotoxicity of those drugs. Fatty Acid Binding Protein 3 (FABP3) is in the FABP protein family that facilities the transport of fatty acids and is in the heart and is hypothesized to interact with P450 2J2 to facilitate the breakdown of drugs. Understanding the interaction between P450 2J2 and FABP3 is necessary for identifying the role FABP3 plays insequestering or transferring substrates for P450 2J2 during heart failure. By using fluorescence titrations, the Guengerich lab has elucidated new ligands with micromolar binding to FABP3. These new structures included palmitate (3 nM[FG1.1]), mefenamic acid (3.4 µM[FG2.1]), tolfenamic acid (1.4 µM), and rivaroxaban (0.84 µM). By finding new ligands of FABP3, further studies can be designed to determine how FABP3 and P450 2J2 interact and thereby define potential relationships between drugs and cardiac cytotoxicity.

Bio. Isabella Dennison is a rising senior at Grove City College pursuing a major in Biochemistry and is concentrating in molecular biology. Isabella’s research journey goes back almost 5 years to the Project Lead the Way Biomedical Sciences program where she conducted college-level research that was used for her capstone project. Additionally, in high school, she studied at Walsh University with a professor studying the effects of single nucleotide polymorphisms on Pax6 protein structure and its contribution to the development of ADHD. In the summer of 2025, she was at Yale University where she was a summer student in the School of Public Health studying genome wide association studies in oysters and was also involved in the Yale RNA club. She is currently a member of the Kriley Crystallography laboratory and has been for 2 years. She currently works on devising synthetic routes for closed ring chalcogens where she applies them to cancer cells to observe their apoptotic effects. Her group’s work has been presented at regional and national ACS conferences. Isabella is studying in F. Peter Guengerich’s laboratory focusing on how the cytochrome P450 2J2 pathway impacts the development of cardiotoxicity through its interactions with FABP3. Isabella is also a member of the BBB honorary, co-founder and Vice President of the disability outreach club, and an ACS member and ambassador for her college. She hopes to pursue a Ph.D. in biochemistry and molecular biology, hoping to study RNA and post-transcriptional regulation. Isabella hopes to become a professor someday and wants to contribute to the world’s scientific knowledge.

Feyza Horuz

Mentor: Michael Stone
Home Institution: Wesleyan University 

"Structural and Thermodynamic Characterization of Ametantrone-AP Site DNA Conjugates"

DNA alkylation at N7-dG generates apurinic/apyrimidinic (AP) sites, which equilibrate between α and β anomers via a transient aldehyde intermediate.Ametantrone (AMT), 1,4-bis[2-(2-hydroxyethylamino)ethylamino]anthracene-9,10-dione, a chemotherapeutic DNA intercalator and topoisomerase II inhibitorused to treat lung carcinoma and leukemia, forms conjugates with these AP sites. Its secondary amines react with the aldehyde intermediate to form a reversible Schiff base, which may be reduced to isolate a stable AMT-AP conjugate. This study aims to structurally characterize the AMT-AP conjugate andits effect on DNA duplex thermodynamics. We synthesized the AMT-AP conjugate, purifying it by reverse-phase HPLC, desalting, and hydroxyapatite chromatography, and confirmed successful synthesis by MALDI mass spectrometry. We examined the thermodynamic stability and structural changes of the AMT-AP conjugate relative to the analogous mitoxantrone-AP (MTX-AP) conjugate and the unmodified duplex. Preliminary melting temperature (Tm)data revealed that the AMT-AP duplex had a Tm of 40°C, compared to 47°C for the MTX-AP duplex and 52°C for the unmodified duplex, indicating that AMT conjugation is more thermodynamically destabilizing than MTX conjugation. To investigate the structural basis for this destabilization, we perfor med 2D COSY and NOESY NMR spectroscopy on the AMT-AP duplex across a range of temperatures (278–298 K). This analysis suggests that AMT conjugation substantially disrupts duplex structure, with distortion increasing as the temperature rises. These findings offer insight into the structural andthermodynamic components of AMT conjugation to an AP site.

Bio.  Feyza Horuz is a rising junior at Wesleyan University majoring in Molecular Biology and Biochemistry. As a McNairScholar, she is part of a federal program supporting first-generation, low-income students pursuing graduate study. She is currently conducting research in Dr. Michael P. Stone's lab under graduate students Nourhan Aboomar and Jason Chapin,studying how the anticancer compound ametantrone structurally impacts the DNA duplex. At Wesleyan, she works in the Holmes lab investigating the autoregulation of linker histone H1 and serves as a biology editor for the Wesleyan ScienceJournal. She is also active on the executive board of the Muslim Students Association as the Communications andOutreach coordinator and competes with Wesleyan's women's club soccer team and Taekwondo group. Feyza is pursuing a PhD and is actively exploring possible avenues for her future studies, with interests spanning molecular biology, biochemistry, cancer biology, and chemical biology.

Songhyun Kim

Mentor: Allison Walker
Home Institution: Colorado College

The rise of antibiotic-resistant bacteria has created a need for new antibacterial compounds, particularly those with novel structures. However, conventionalscreening of laboratory monocultures often leads to the repeated discovery of known compounds and fails to fully exploit the biosynthetic capacity of many microbes. Genome sequencing has revealed that numerous bacteria possess multiple biosynthetic gene clusters (BGCs) that are completely silent under standard culture conditions. Co-cultivation of different microbial species is a useful strategy to induce these silent pathways. Pseudomonas putida and Jiangella alkaliphila are both soil bacteria. A co-occurrence network is a graphical network representing relativity between bacteria. Co-culturing these two organisms offers an opportunity to study how interactions between closely associated bacteria influence secondary metabolism and to identify cryptic antibacterial products that are not produced when each strain is grown in monoculture. Our bioactivity assay findings demonstrated antibacterial activityfrom the co-cultivation of two different microbial species, supporting our hypothesis and revealing the potential of awakening cryptic pathways. In addition, LC-MS data showed us future direction in discovering new or unknown molecules. Further research may contribute to the discovery of new antibacterialproducts and provide insight into the biochemical regulation of secondary metabolite production.

Bio.  Songhyun Kim is a rising senior at Colorado College, where she is pursuing a major in biochemistry. She is particularly interested in discovering natural products to develop dermatology products. At Colorado College, she is working on ongoing research on natural fragrance and cosmetic formulation by conducting chemical characterization of essential oils from indigenous and ecologically significant plants from the Southwest region in the U.S.

Jimmy Lin

Mentor: Alexander Schuppe
Home Institution: Amherst College

"Progress Towards the Total Synthesis of Andiconin B"

3,5-Dimethylorsellinic acid (DMOA)-derived fungal meroterpenoids represent a diverse class of hybrid polyketide–terpenoid natural products. They have a wide range of biological benefits, including anti-inflammatory, antibacterial, and anticancer, making them a highly desirable product in medicinal chemistry. Furthermore, their densely functionalized polycyclic framework, with multiple contiguous and quaternary stereocenters, contributes to their structural complexities, making them attractive yet challenging targets for organic synthesis. Andiconin B is a complex fungal meroterpenoid consisting of a 6/6/5/6/5 pentacyclic bridged-ring framework embedded with multiple quaternary stereocenters, which present significant synthetic challenges. This project aims to work towards the total synthesis of andiconin B from commercially available geraniol. Key transformations include a one-carbon homologation via a cascade of allylic oxidation and Wittig olefination, followed by a one-pot hydroboration of the resulting polyene with 9-BBN and a Suzuki-Miyaura cross-coupling toconstruct the extended carbon structure, thereby establishing the molecular framework necessary for a future polyene cyclization to yield the characteristic meroterpenoid core. The development and optimization of this pathway will provide an efficient and scalable synthesis route towards andiconin B and other structurally similar meroterpenoids. Beyond contributing to the advancement of synthetic methodology applicable to complex natural products, this work will support future research in medicinal chemistry and natural product discovery.

Bio.  Jimmy Lin is a rising senior at Amherst College, majoring in Biochemistry & Biophysics. At Amherst, heconducts research in the Carter Lab, where he studies viral genomic folding dynamics by the SARS-CoV-2 nucleocapsid protein. His research aims to investigate the role of non-covalent interactions between the viralgenome and proteins to elucidate the mechanism of DNA folding. He has also conducted research at the University of Hartford, where he studied viral membrane proteins using computational techniques to decipher how the local microenvironment of the amino acids affects their biochemical behavior. This summer, he is an REU intern in the Schuppe Lab at Vanderbilt University, where he is working toward the total synthesis ofandiconin B. After graduation, he intends to pursue a Ph.D. in chemistry with a focus on organic synthesis.

Grant Mentzer

Mentor: Jeffrey Spraggins
Home Institution: The College of Wooster 

"A Multi-omics Workflow for Mapping the Staphylococcus aureus Biofilm using Matrix-Assisted Laser Desorption/Ionization Imaging Mass Spectrometry"

Staphylococcus aureus is a widespread bacterial pathogen possessing an array of virulent adaptations. One is antimicrobial resistance, which is responsible for S. aureus’s prevalence in society despite advances in antibiotics. Also contributing to S. aureus virulence is its ability to form biofilms, large secretions ofpolymers, that protect the bacteria from mechanical stress and help sequester and retain nutrients. In addition, S. aureus is a facultative anaerobe whichgrants it the ability to acclimate to environments of varying oxygen concentration. In lieu of these adaptations, there is a demand for imaging approaches thatcan provide a new perspective on the mechanisms behind S. aureus virulence. Matrix-assisted laser desorption/ionization imaging mass spectrometry (MALDI-IMS) is an imaging technique that has been used to spatially map the molecular make-up of S. aureus biofilms, revealing new insights into S. aureus biology. Providing comprehensive molecular coverage of the S. aureus biofilm with spatial resolution is important to help understand the pathologicalmechanisms involved in human infection. In this study, we utilized a workflow that prepares representative cross-sections of the S. aureus biofilm that provide3-dimensional molecular and spatial information. Biofilms underwent cryosectioning in 50-100 µm intervals, a series of washes and matrix applications, then MALDI-IMS acquisition. We collected MALDI-IMS data that covers metabolomic, lipidomic, and proteomic features relevant to S. aureus pathology. Oursample preparation methodology allowed for lipidomic and proteomic acquisition to be performed on the same section. Featured detected molecules includemetal-sequestering siderophores Staphyloferrin A and B, heterogenous lipid layers implicated in antimicrobial resistance, and cytolytic peptide δ-hemolysin, all implicated in S. aureus virulence. Our work provides a method to spectrally and spatially detect a wide range of biomolecules in the S. aureus biofilm,allowing for the comparison of interrelated biological mechanisms contributing to the devastating effects of S. aureus infection.

Bio.  Grant Mentzer is a rising junior at The College of Wooster currently pursuing his degree in chemistry. Whether it be identifying biomarkers of disease or revealing new insights into the nuances of metabolism, Grant has an interest in applying analytical techniques to answer questions in biology. Previously, He has done research at Wooster under Dr.Mark Snider, working to elucidate the mechanism behind 6-hydroxynicotinate 3-monooxygenase, a bacterial enzyme in the nicotinic acid degradation pathway, using UV/vis kinetics methods. Grant was also a participant in the 2025 Ohio State University ORIP cohort, where he worked on a methodology for the detection for bacterial plant pathogens under Dr. Francesca Rotondo. In addition to research at Wooster, Grant has worked as a teaching assistant for molecularbiology and general chemistry courses, works for Wooster Community Hospital as a student Health Coach, is a member of the varsity cross country and track and field teams, and plays in a student-led jazz band.

"Rpl23-snR35 Model of Interaction for Oxidative Stress Response"

Eukaryotic ribosomes are composed of 79 ribosomal proteins (RPs) and 4 rRNAs that function to translate RNA to polypeptide chains. Under stressconditions in yeast, RPs altered by stress can be removed from ribosomes chaperone proteins. Rpl23 is an RP located on the 60S ribosomal subunit, whichis taken off the ribosome under oxidative stress conditions by Bcp1, and in human cells, this free Rpl23 binds the human ortholog of snR35, a small nucleolarRNA that is necessary for modification and folding of the 18S ribosomal RNA during biogenesis. We hypothesize that under oxidative stress conditions, the snR35 diversion occurring due to its interaction with free Rpl23 may aid cells in adapting to and surviving the stress, despite it preventing snR35 from performing its vital role in 40S subunit biogenesis. Given that ribosomes and their translation of RNA into proteins are severely impacted under oxidative stress, translation regulation must be adjusted to concentrate the cell’s efforts toward functions that will help adapt to the stress and survive. In this study, weused an AlphaFold of Rpl23 and snR35 to produce five mutant Rpl23 plasmids that would be defective in binding to snR35, while still maintaining connections with the 60S subunit and Bcp1. We then completed several growth curves and viability assays that established phenotypes for these mutants.We discovered that the mutations I37G and W85A mutants provided significant growth defects in the yeast, consistent with the mutation interfering withRpl23’s interaction with the 60S subunit or Bcp1. Meanwhile, the other mutants, K64A, R70A, and RRR86-88AAA, showed little to no growth defects, indicating either alteration to Rpl23’s interaction with snR35 or no effect. Excitingly, we found that the I37G mutant abolished an established growth defect produced by Rpl23 overexpression, which we suspect is due to interrupted interaction with snR35. Furthermore, both deletion of snR35 and overexpression of WT Rpl23 produce synthetic sick effects when the ribosomal proteins nearby to snR35 are mutated. We are currently completing in vitro RNA-bindingassays to confirm the Rpl23-snR35 interaction and will repeat these with our promising I37G mutant.

Bio.  Kaydra Osmundson is a rising junior at Ball State University, majoring in Chemistry with a Biochemistry concentration, with minors in Spanish and Physiology. At her home institution, she is conducting research in Robert Sammelson’s organic chemistry lab, working on synthesis of an analog to the natural product Ipomoeassin F, which has been found to have potent cytotoxicity to tumor cells. Next semester, Kaydra will besharing her love of biochemistry and its critical roles as an SI (supplemental instruction) leader in Cell Biology andas secretary of Ball State’s Student Affiliates of the American Chemical Society (SAACS) Club. She also seeks tohelp the community through participation in the Honors Association for Community Engagement, which she is excited to lead next year as President. In her free time, Kaydra loves to dance, read, crochet, and go on hikes. Forher future career, Kaydra hopes to conduct biochemical research that will substantially contribute to advancements in medicine.

Cameron Page

Mentor: David Cliffel
Home Institution: James Madison University 

"Human Milk Oligosaccharides Modulate Interleukin-1 Secretion in a Preterm Birth Context"

Human milk oligosaccharides (HMOs) are structurally diverse carbohydrates that demonstrate antimicrobial and antibiofilm properties against pathogens that are a major cause of preterm birth (PTB), such as Group B Streptococcus (GBS). Inflammatory cytokines, such as Interleukin-1b (IL-1b), are biomarkers of PTB. Recent studies suggest HMOs demonstrate immunomodulatory effects on inflammatory cytokine secretion. Magnetic bead electrochemical sandwich assay (MBESA) is an electrochemical biosensor method that leverages the reduction-oxidation reaction of 3,3’,5,5’-tetramethylbenzadinie and horseradish peroxidase to produce amperometric signal, providing a rapid and sensitive alternative to conventional enzyme-linked immunosorbent assay (ELISA) methods for quantifying cytokine levels. In this study, MBESA was utilized to optimize a biosensor to quantify IL-1b secretion in THP-1 macrophages that were subjected to GBS infection and HMO treatment at three treatment timepoints and three HMO doses. An assessment was also made based on pre or post treatment with HMOs, compared to a coadministration of HMOs and GBS. In this study, HMOs exhibited a dose dependent effect on IL-1b secretion in THP-1 macrophages in baseline and GBS-induced secretion. Pre treatment with HMOs suppressed IL-1b secretion compared to cotreatment of HMOs andGBS at the equivalent timepoint. These findings highlight the potential for utilizing HMOs as therapeutic agents for treating inflammatory-related diseases. Future work will work towards further quanitfying other cytokines, such as Interleukin-6 (IL-6), and integrating optimized MBESA sensors with a fetal membrane on-a-chip model (FMOC) to further investigate the therapeutic capability of HMOs in reproductive health.

Bio.  Cameron Page is a rising senior at James Madison University in Harrisonburg, Virginia where she is earning a B.S. in chemistry with a concentration in biochemistry. At James Madison, Cameron conducts research in the Macdonald lab studying the effects of Hofmeister series ions on caffeine solvation and water structure. She is also an active member of Beta Beta Beta Biological Honors Society and Iota Sigma Pi Honors Society chapters at James Madison. Cameron has spent her summer at Vanderbilt University in the Cliffel lab researching the immunomodulatory effects of human milk oligosaccharides on inflammatory cytokine secretion in THP-1 macrophages. After graduating, Cameron plans to pursue a Ph.D. in chemistry.

Matthew Poppitz

Mentor: Daria Kim
Home Institution: Emory University

"Redirecting Carboxyl Radical Reactivity through Associative Proton-Coupled Electron Transfer"

Carboxyl radicals are widely used in organic synthesis as convenient precursors to C-centered radicals due to their inclination for rapid and favorable decarboxylation (ca. k = 10⁹s^-1). While this reactivity has enabled the development of decarboxylative functionalization chemistry, non-decarboxylative transformations of aliphatic carboxyl radicals remain exceptionally rare because decarboxylation readily outcompetes other reactivity pathways. Herein, we report an intramolecular alkene lactonization reaction through carboxyl radicals enabled by a proton-coupled electron transfer (PCET) strategy that prevents decarboxylation through hydrogen-bonding association. We have recently developed a bifunctional organophotocatalyst by covalently linking a xanthone photooxidant and a phosphate base, to promote O-H bond homolysis. We propose that the hydrogen-bonding association could stabilize the newly generated carboxyl radical species to prevent classical carboxyl radical decarboxylation and allow for irreversible radical cyclization (ca. k = 10⁶s^-1), providing direct access to anti-Markovnikov lactones from alkene-containing carboxylic acids. Control experiments demonstrate that preorganization of the photooxidant and phosphate base via covalent linking is necessary for this reactivity, whereas analogous decoupled catalyst systems exhibit low conversion. Complementary reaction manifolds were identified, including conditions that exploit reversible hydrogen atom transfer with chloroform to further preserve the carboxyl radical in highly fragmentation-prone tertiary positions. This enables cyclization across a broad range of primary, secondary and tertiary aliphatic carboxylic acids that would otherwise undergo rapid decarboxylation. More broadly, this work demonstrates that associative PCET can redirect the intrinsic reactivity of carboxyl radicals, providing access to non-decarboxylative reaction pathways that have previously remained inaccessible.

Bio.  Matthew Poppitz is a rising senior at Emory University majoring in Chemistry, with research interests in synthetic organic chemistry, catalysis, and reaction development. He conducts research in Dr. Huw Davies’ lab, working on rhodium-catalyzed C–H functionalization for new C-C bond-forming methods. Outside the laboratory, Matthew serves as Director of the Emory-Tibet Science Initiative Peer Mentoring Program, part of an educational partnershipestablished with His Holiness the Dalai Lama to incorporate modern scientific knowledge and methodology into theTibetan monastic tradition. He works directly with Tibetan monastic scholars and Emory faculty, supporting both classroom learning and laboratory research. Following graduation, he hopes to pursue a Ph.D. in organic chemistry and a career in pharmaceutical research and development.

Malena Saporito

Mentor: Nathan Schley
Home Institution: Auburn University

"Borylation of 1,1-difluoroethane and Applications in Allylic Cross Couplings"

Carbon-boron bonds are notable for their versatility in organic synthesis and are highly valued in synthetic medicinal chemistry and materials science. Ourlab is interested in the use of the undirected borylation of alkanes as a way to access this valuable motif. 1,1-difluoroethane is commonly used as apropellent in canned air products and as such, is uniquely affordable. This availability inspired us to use difluoroethane as a substrate for borylation in aneffort to develop a method for the incorporation of the difluoroethyl fragment into drug-like molecules. Our chosen method is an undirected borylation followedby a cross-coupling of the resulting nucleophilic alkyl boronic ester into an allylic electrophile. For the borylation, we used an iridium catalyst paired with our lab‘s signature dipyridylarylmethane ligands and for the allylic cross coupling, we plan to use an iridium catalyst along with a phosphoramidite ligand. Saidsubstrates and ligands were synthesized. Results were determined and analyzed through ¹H NMR and GC-MS. Products were purified via distillation and column chromatography. 1,1-difluoroethane was successfully borylated with bis(pinacolato)diboron and substrates for cross-coupling with the borylated fluoroalkane are currently being prepared, starting with the Boc protected 1-phenyl-2-propen-1-ol. We are hopeful that we will be able to synthesize thedifluoroethylated benzylic alcohol. Future research will be aimed at the optimization of the allylic cross coupling, as well as development of a larger substratescope. We predict this reaction will open avenues for other interesting reactions in the future. This project will be continued after the conclusion of this REU by Ph.D. student Ezekiel Mulder.

Bio.  Malena Saporito is a rising junior transferring to Auburn University, majoring in Chemical Engineering. She completed herfirst two undergraduate years at Volunteer State Community College, achieving her Associates of Science in Chemistry simultaneously with her high school diploma. She is interested in large-scale pharmaceutical manufacturing and aims to enter the industry in two years after completing her Bachelor of Chemical Engineering with a concentration in Biochemical Engineering.