Summer Fellows in Chemistry and BCMB

This year, nine students worked with five chemistry professors on Summer Fellows research projects. Take a look at these exciting projects:

 

Kara DiJoseph (Biology ’14) is working with Dr. Mark Ellison to find ways to use carbon nanotubes to overcome bacterial resistance to antibiotics. She is attaching tetracycline to carbon nanotubes and studying the effectiveness of these modified nanotubes at killing normal and antibiotic-resistant E. coli. Kara will present her results at the ACS National Meeting in Philadelphia in August and continue her research during the school year.

 

 

Caitlin Galvin (Chemistry ’13) continued her work on the characterization of an octyl HPLC stationary phase. In this work she has been determining the thermodynamics of the retention process while using a mobile phase composition of 10% methanol, 90% water. In addition to looking at differences in her own dataset, she compared her results to those obtained previously in the group using different stationary and mobile phase compositions. In addition, Caitlin laid the groundwork for work that she will continue during the school year by doing the initial work using the LC/MS and learning about multivariate analysis techniques. Caitlin will present her work at the ACS National Meeting in Philadelphia in August and in regional meetings during the school year.

 

Chris Goodwin (BCMB ’13) is working with Dr. Mark Ellison to attach antiviral drugs to carbon nanotubes to improve drug delivery. He is attaching acyclovir to carbon nanotubes to test its effectiveness at delivering the drug to Herpes-Simplex-virus-infected cells. Chris also studied the toxicity of nanotubes toward C. elegans. Chris will present his results at the ACS National Meeting in Philadelphia in August and continue his research in the fall as an Honors project.

 

Kelechi Iro Kalu (Neuroscience ‘13) is working with Dr. Julia Koeppe on a project to investigate the interaction between complement factor 3 and thrombomodulin. Thrombomodulin is a protein best known for regulating blood clotting, but it has recently been implicated in interfering with inflammation via the innate immune response. Kelechi will be isolating and purifying complement factor 3 from blood plasma, expressing and purifying thrombomodulin from yeast and then developing a pull-down assay to study the interactions between the proteins.
Nicholas Nobiletti (BCMB ’13) is working with Dr. Julia Koeppe to investigate interactions between inflammation and coagulation. Nick is expressing the protein thrombomodulin in yeast, purifying this protein by FPLC (fast protein liquid chromatography), and then analyzing it by protease cleavage and mass spectrometry. Nick is also working with purified complement factor 3, and he will be investigating interactions between this protein and thrombomodulin by mass spectrometry in the fall and spring semesters.

 

With the goal of learning more about structure-function relationships in di-iron carboxylate proteins, Connor Kanya (Chemistry ’14) and Dr. Amanda Reig are working to create small, protein-based models that mimic the active sites of two natural enzymes: FprA and MIOX. The structures of these two enzymes have recently been elucidated and show a unique combination of 4 histidine and either 2 or 3 carboxylate residues in the active site. The basis for their model is a previously designed de novo protein that contains 2 histidine and 4 carboxylate residues. Their summer research will involve site-directed mutagenesis to alter the model protein active site followed by production, purification, and characterization of the new model protein.

 

What did Jonathon Birabaharan, Hongli Chen, and Danielle Miller (all BCMB majors, Class of 2014) do this summer? Working with Professor Codrina Popescu as their
mentor, they studied the enzyme dehaloperoxidase (DHP) from the marine worm Amphitrite ornata, a project funded by an NSF grant to Dr. Popescu. Dehaloperoxidase is the first hemoglobin with significant peroxidase activity, which is used by the worm to oxidize toxic halophenols. Given the flexibility of the active site, we hypothesize that this enzyme could oxidize a variety of substrates that share some structural similarity with the native substrate, triiodophenol. This year’s summer fellow projects are exploring the potential binding and catalytic activity of DHP towards common environmental aromatic pollutants, such as BPA and certain polychlorinated aromatics. In addition we are studying the proposed catalytic cycle of DHP with Mössbauer spectroscopy, aiming to characterize high-valence intermediates.The three students will accompany Dr. Popescu at the National ACS meeting in Philadelphia, this August (2012) to present the reults of their work.”

 

Comments are closed.