Synthesizing proteins containing unnatural amino acids inserted at specific positions within the protein sequence has been a longstanding goal of biological chemists. This poses unique challenges, as aminoacyl tRNA synthetases, the enzymes responsible for protein synthesis, are highly specific. To overcome this, a lanthanum-catalyzed, biomimetic tRNA aminoacylation method has been developed(1). However, due to unproductive lanthanum coordination of ethyl phosphate, a reaction byproduct, a full equivalent of lanthanum must be added to each reaction. This may threaten the integrity of tRNA, as lanthanides are known to catalyze the hydrolysis of RNA (2, 3). Using uridine as a simplified tRNA mimic, magnesium, which is known to coordinate strongly with phosphate ions, has been utilized to optimize this reaction and increase the selectivity of lanthanum towards esterification. In the presence of magnesium, ester yield is substantially increased. In addition to this, optimal pH and buffer reaction conditions were determined.
| Identifer | oai:union.ndltd.org:TORONTO/oai:tspace.library.utoronto.ca:1807/18224 |
| Date | 05 January 2010 |
| Creators | Bunn, Shannon Elizabeth |
| Contributors | Kluger, Ronald |
| Source Sets | University of Toronto |
| Language | en_ca |
| Detected Language | English |
| Type | Thesis |
Page generated in 0.0021 seconds