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2008 Proceedings - St. Cloud State University

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Abstracts<br />

Session A All Disciplines Ballroom<br />

Development of Gas Chromatography Mass Spectrometry and High Performance Liquid Chromatography Methods for the<br />

Detection of Ethylene Glycol Ethers<br />

Ethylene glycol ethers (EGEs), especially 2-ethnoxyethanol and 2-butoxyethanol (BE) are excellent solvents. Accordingly, they are used in<br />

many industrial and commercial products. Upon human use, these solvents are discharged into waterways. Given the use and discharge<br />

of EGEs, both humans, as well as aquatic animals are exposed to EGEs. Exposure to EGEs results in various toxicities including<br />

encephalopathy, hemolysis and metabolic acidosis in humans. In addition to these toxicities, carcinogenesis and mutagenesis is also<br />

observed in animal models. Actual concentrations of EGEs in waste water discharges are not clearly established accordingly. The<br />

objective of this research project is to develop a method to determine the presence of butoxyethanol (BE), one of the most common EGEs<br />

used, and its possible metabolites butoxyacetaldehyde (BAL) and butoxyacetic acid (BAA) in waste water sample. The group is currently<br />

standardizing a gas chromatography mass spectrometry method for this purpose and is in the process of developing a high performance<br />

liquid chromatography method.<br />

Presentation Index: A57<br />

Time: 9:00 a.m.<br />

Department: Chemistry<br />

Project Sponsor(s):<br />

<strong>St</strong>udent Presenter(s): Cheng, Shiang Kai<br />

Sreerama, Lakshmaiah<br />

Mechanism of Action of Alzheimer’s Disease Drugs on the Aggregation of Amyloid Beta Peptide<br />

Alzheimer‘s disease (AD) is characterized by the deposition of amyloid â peptide (Aâ) plaques in the brain. Aâ is physiologically produced<br />

from enzymatic cleavage of the larger precursor called amyloid precursor protein (APP). Aâ in its soluble form is not toxic to brain cells<br />

(neurons); however its aggregation into insoluble fibrils which then combines with cell debris to form plaques causes neurotoxicity. Since<br />

the aggregation of Aâ peptide to insoluble fibrils is due to their hydrophobic interaction, it is proposed that small chemical compounds<br />

which are hydrophobic might inhibit the hydrophobic interaction between amyloid peptides, hence inhibiting the formation of insoluble fibrils<br />

which precedes the plaque formation. The proposed research is to see how hydrophobic drugs, which are currently used for treating AD<br />

patients, such as Galantamine, Memantine and Tacrine affect the formation of amyloid aggregates. Thioflavin T (ThT) dye will be used to<br />

study the aggregation of peptides as the dye has very good affinity with aggregated peptide. It is proposed that greater the aggregation of<br />

amyloid peptide greater will be the fluorescence intensity of the dye and in the presence of drugs that inhibit the aggregation of the peptide<br />

fluorescence intensity of the dye will decrease. The study of fluorescence intensity as a function of different concentration of drug will show<br />

which drug is most effective in inhibiting aggregation of amyloid peptide. The most effective drug could be used as a potential molecular<br />

framework for designing new improved drugs with fewer side effects to treat AD.<br />

Presentation Index: A58<br />

Time: 9:00 a.m.<br />

Department: Chemistry<br />

Project Sponsor(s):<br />

<strong>St</strong>udent Presenter(s): Henning, Phillip; Bhattarai, Nirjal<br />

Ramakrishnan, Latha<br />

Mad Protein Under-Regulation or Over-Expression Outside The Nucleus: A Possible Cause for Adenocarcinoma Breast Cancer<br />

Cell Resistance to Ottelione A<br />

In the world, breast cancer is the fifth leading cause of cancer related death after lung, stomach, liver and colon cancer. By the end of this<br />

year, breast cancer is expected to cause 40,910 deaths (7% of all cancer deaths, almost 2% of all deaths) in the U.S alone. One of the<br />

biggest problems in the treatment of cancer today is drug resistance. Therefore, research on anti-cancer drug resistance is very important<br />

in finding treatment for cancer. This research will focus on finding out why cancer cells, breast cancer cells in particular, are resistant to the<br />

anti-cancer drug, Ottelione A (OttA). Recent research has shown that Ottelione A is a very potent anticancer drug that inhibits tubulin<br />

polymerization. OttA blocks cell division at the metaphase/anaphase junction of mitosis and triggers the signal cascade, prompting<br />

programmed cell death (apoptosis). The mechanism by which OttA inhibits tubulin polymerization is unknown. Human breast<br />

adenocarcinoma MCF 7/0 cells are wild type tumor cells sensitive to OttA. MCF 7/OttA cells (sub-line of human breast adenocarcinoma<br />

MCF 7/0) are relatively insensitive to OttA. Genomic Analysis of MCF 7/O and MCF 7/OttA cells have shown that > 50 genes are differently<br />

expressed in MCF 7/OttA cells compared to MCF 7/0 cells. This observation has further led to the hypothesis that OttA drug resistance is<br />

due to the down-regulation and/or over-expression of mitotic arrest deficient (MAD) proteins, MAD1 and MAD2 outside the nuclei.<br />

Therefore, this research will investigate the mis-localization of MAD1 and MAD2 proteins outside the nuclei.<br />

Presentation Index: A59<br />

Time: 9:00 a.m.<br />

Department: Chemistry<br />

Project Sponsor(s):<br />

<strong>St</strong>udent Presenter(s): Mususu, Muchima<br />

Sreerama, Lakshmaiah<br />

<strong>St</strong>. <strong>Cloud</strong> <strong>St</strong>ate <strong>University</strong> <strong>St</strong>udent Research Colloquium 34<br />

April 22, <strong>2008</strong>

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