Date of Graduation

Summer 2021

Degree

Master of Science in Chemistry

Department

Chemistry and Biochemistry

Committee Chair

Keiichi Yoshimatsu

Abstract

In this thesis, I report the preparation and characterization of dye-containing PEG-b-PLA block copolymer micelles and the computational design of a novel coiled-coil peptide bundle. The PEG-b-PLA micelles encapsulate hydrophobic molecules into their core and have strong potential as nanocontainers or delivery vesicles. In theory, these internalized molecules can be released upon exposure to mechanical forces that disrupt the micellar structures. This force-responsive nature is one of the inherent properties of micellar systems. However, there is a stark lack of research that utilize this property in applications. Along those lines, I have studied the behavior of dye-containing micelles upon exposure to mechanical stresses. In this work, two fluorescent dyes that undergo fluorescence resonance energy transfer (FRET) in close proximity have been used as reporters to gauge the structure of the micelles. Upon exposure to mechanical force via vortexing, the fluorescent signal of micelles decreases as a function of rotational speed and time of vortexing. In another project, I have worked on the design of a novel coiled-coil peptide bundle. Coiled-coil peptides have been widely used as templates for protein design. The specific goal of this project was to develop a photo-responsive hexameric coiled-coil bundle that can incorporate hydrophobic molecules into the interior core and reversibly catch and release small molecules. The azobenzene derivative, BSBCA was chosen as the linker to impart the photo-responsive properties to the peptide bundle. Using the PyRosetta computational suite, I have identified 3 top candidates of the mutated peptides that contain two cysteine residues to be linked with BSBCA and are anticipated to form stable hexamer bundles in aqueous environment.

Keywords

force responsive materials, FRET, block copolymers, self-assembly, coiled-coils, protein design, stapled peptides

Subject Categories

Biochemistry | Other Chemistry | Polymer Chemistry

Copyright

© Tyler L. Odom

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