Journal of Undergraduate Research
Keywords
cyclic peptide, catalyst, enzymes
College
Physical and Mathematical Sciences
Department
Chemistry and Biochemistry
Abstract
Enzymes found in nature are more efficient catalysts than those used in organic chemistry labs. However, natural enzymes are not ideal for organic synthesis because they only make one product and only work in specific conditions. The Michaelis lab designed a catalyst capable of mimicking enzyme-like reactivity in the lab. This catalyst consists of an alpha helix with an imidazolidinone catalyst and a thiourea catalyst (see figure 1). The imidazolidinone catalyst and thiourea catalysts are attached adjacent to each other on the alpha helix, which acts as a rigid scaffold that can mimic the proximity effects seen in natural enzymes. In the past, we have shown that this alpha helical catalyst can catalyze a Diels-Alder reaction, which is important to pharmaceutical research, faster than other catalysts. In the past few months, we have also attached a TEMPO catalyst to the alpha-helical scaffold. This catalyst is currently used only in academia because it is too expensive to use on large scales needed in industry. Attaching it to our alpha helical scaffold would increase the recyclability of the TEMPO catalyst and reduce its cost.
Recommended Citation
Campbell, Millicent and Michaelis, David
(2019)
"Cyclic Peptide Catalyst design,"
Journal of Undergraduate Research: Vol. 2019:
Iss.
2019, Article 147.
Available at:
https://scholarsarchive.byu.edu/jur/vol2019/iss2019/147