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Friday, December 19, 2014 - Hanna Trzeciakiewicz wins Undergraduate Distinguished Achievement Award
Biochemistry major Hanna Trzeciakiewicz was awarded OU’s Undergraduate Distinguished Achievement Award at the fall commencement. The award was presented by interim Vice President of Student Affairs Glenn McIntosh, who said
“The Undergraduate Distinguished Achievement Award was established in 1986 to recognize extraordinary academic accomplishment beyond superior grades. A student’s scholarly publication in the arts, sciences, or a professional field; the creation of performance of an artistic work; or the construction of a device or instrument are representative criteria for this award.

It gives me great pleasure to ask the Undergraduate Distinguished Achievement Award recipient for 2014, Hanna Trzeciakiewicz, to come to the stage. As an undergraduate major in Biochemistry, you have not only maintained a GPA of 3.98, but have done impressive research in your field of study. You are the first author of an article that has been accepted for publication in a peer-reviewed journal, Electrochmica Acta, and co-author of another peer-reviewed work that has appeared in the journal Analyst. You have also made oral presentations and presented posters at the meetings of professional organizations, notably including the American Chemical Society and the International Society of Electrochemistry. As a member of the Oakland University Community, you have been active in several student organizations, including the American Chemical Society—Student Affiliates. You were instrumental in organizing a meeting of this group at Oakland University in the spring of 2014. You have also shared your knowledge of and your passion for biochemistry by tutoring both high school and college students in chemistry, biology, and mathematics. For these accomplishments, we are proud to honor you with the Undergraduate Distinguished Achievement Award for 2014. Congratulations!”
Trzeciakiewicz works in the laboratory of Assistant Professor Sanela Martic, of the Department of Chemistry. Martic and her group of students study interactions between the biomolecules, such as peptides, proteins, DNA and RNA, in solution and on surfaces.

Trzeciakiewicz participated in the Summer Research Program in Biological Sciences and Chemistry, which encourages talented undergraduate students to consider graduate study in biological sciences and chemistry. She also has held the Michael P. and Elizabeth A. Kenny Merit Scholarship for the Sciences, obtained a Chrysler Undergraduate Student Research Award, and is a member of the Honors College.

Trzeciakiewicz’s paper Electrochemistry of Heparin Binding to Tau Protein on Au Surfaces is currently in press in Electrochim Acta. Coauthors include Martic, PhD student Jose Esteves-Villanueva, and MS student Nicholas Carlin. The abstract is given below.
The tau protein is a neurodegenerative disease biomarker. The in vitro aggregation of tau is triggered by electrostatic charge imbalance induced by an anionic inducing agent, such as heparin. The binding of the tau-heparin complex is based on electrostatic interactions, but the exact binding mode of heparin to the tau protein has not been fully identified. In this work, the effects of the tau protein orientation on gold (Au) electrode to heparin were explored by the cyclic voltammetry and electrochemical impedance spectroscopy. To modulate the accessibility of N-terminal of the tau to heparin, the tau films on Au surfaces were fabricated in two ways: immobilization of tau via the N-terminal of tau protein (N-tau-Au) or by the Cys291/Cys322 residues, located in the R-repeat domains of the tau protein (Cys-tau-Au). The sulfur-Au bonding was characterized by X-ray photoelectron spectroscopy. The charge transfer resistance was measured for N-tau-Au and Cys-tau-Au as a function of heparin concentration. The heparin concentration range was varied from 0.2 pM to 216 μM with the optimal binding concentration at 21 nM (the highest charge transfer resistance value). The heparin binding to tau films was investigated in the presence of [Fe(CN)6]3−/4− or benzoquinone redox probes. The tau-heparin binding was greater for the Cys-tau-Au surface over N-tau-Au, indicating specific tau domains may be required for optimal heparin binding.