Science University Research Symposium (SURS)

Publication Date

2026

College

College of Sciences & Mathematics

Department

Chemistry and Physics, Department of

SURS Faculty Advisor

Duane Hatch

Presentation Type

Poster Presentation

Abstract

X-ray crystallography is a widely-used technique for determining protein structures. However, proteins composed mostly of lighter atoms can make structural analysis challenging. Incorporating heavier atoms, such as selenium, into amino acids may improve analysis using crystallography. This project focused on the synthesis and characterization of iodide and selenide intermediates toward the development of seleno-tryptophan, a selenium-containing analog of the amino acid tryptophan.

An iodide intermediate was first synthesized through a Finkelstein reaction and then used in the synthesis of a selenide intermediate. Reaction progress and product formation were monitored using thin-layer chromatography (TLC) and nuclear magnetic resonance (NMR) spectroscopy. NMR analysis supported the successful formation of the iodide intermediate and provided evidence for the formation of the selenium-containing product. However, the selenide product was only partially purified, and residual starting materials and impurities were observed. Future research will focus on optimizing reaction conditions and purification methods to improve product yield and purity. These findings represent progress toward the synthesis of seleno-tryptophan and its potential application in crystallographic protein structure analyses.

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