Recognition of nucleotides and peptides using designed betahairpin peptides and dynamic combinatorial chemistry Public Deposited

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Last Modified
  • March 21, 2019
Creator
  • Cuellar, Matthew E.
    • Affiliation: College of Arts and Sciences, Department of Chemistry
Abstract
  • Non-covalent interactions contribute to the stability and formation of biomolecules, e.g. proteins, DNA, and RNA. More relevant to this dissertation, they also contribute to the interaction between these biomolecules, e.g. protein-protein, protein-RNA, and protein-DNA interactions. This work describes the use of model systems (peptide and small molecule) to mimic protein-RNA and protein-protein interactions. This dissertation is divided into three parts. The first part describes the attempted use of designed beta-hairpin peptides to selectively bind 7mGTP. Despite attempts using different binding techniques (fluorescence titration, microcalorimetry, and NMR titration), the binding of 7mGTP by the beta-hairpin peptides could not be quantified. The second part describes the use of designed beta-hairpin peptides for recognition of polyproline (PPII) helices in a model system. This work demonstrates the use of disulfide exchange to investigate non-covalent interactions in a peptide model system. The third part describes the development and the use of dynamic combinatorial chemistry (DCC) mediated by disulfide exchange. The development of analytical methodology using ultra performance liquid chromatography coupled with mass spectrometry analysis (UPLC/MS) is described. DCC was used to synthesize and identify receptors for both nucleotides and peptides containing a lysine residue with different methylation states.
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  • In Copyright
Advisor
  • Waters, Marcey
Degree granting institution
  • University of North Carolina at Chapel Hill
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  • Open access
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