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The current methods of drug delivery prove to have inefficiencies as far as drug administration to the target site. Due to adverse factors that the drug faces within the body, it can be broken down before the therapeutic can be applied. Polymeric micelles have shown promising results in the face

The current methods of drug delivery prove to have inefficiencies as far as drug administration to the target site. Due to adverse factors that the drug faces within the body, it can be broken down before the therapeutic can be applied. Polymeric micelles have shown promising results in the face of these circumstances, by being able to self-assemble into a core-shell structure to better house the medicine as it travels through blood stream upon intravenous injection. The triblock copolymer, PEG-PPG-PEG, uses it hydrophilic and hydrophobic components to form a spherical micelle at a nanoscale size allowing it cross barriers with greater ease and prolong dissociation. The resulting size of the micelle is measured by the use of a dynamic light scattering machine. Stability factors, such as, thermodynamic and kinetic stability, also aid in the formation of micelles, but are generally effected in drug delivery process by factors such as salt concentration and pH. Both these factors can cause a lack of stability resulting in aggregation of the micelles; therefore, their affects need to be prolonged in order to have sufficient drug delivery.
ContributorsNelson, Adriana Elisabeth (Author) / Green, Matthew (Thesis director) / Nannenga, Brent (Committee member) / Chemical Engineering Program (Contributor) / Barrett, The Honors College (Contributor)
Created2017-05
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Description
Genetically encoded non-canonical amino acids (NCAAs) have allowed researchers to access functionalities that would be otherwise unavailable with the naturally-occurring amino acids. The metal-chelating NCAA (2,2'-bipyridin-5yl)alanine (Bpy-ala) has recently been employed, in tandem with computational modeling, to drive the assembly of a homotrimeric protein complex in the presence of a

Genetically encoded non-canonical amino acids (NCAAs) have allowed researchers to access functionalities that would be otherwise unavailable with the naturally-occurring amino acids. The metal-chelating NCAA (2,2'-bipyridin-5yl)alanine (Bpy-ala) has recently been employed, in tandem with computational modeling, to drive the assembly of a homotrimeric protein complex in the presence of a metal ion, specifically Fe(II). While a successful design was identified to form a homotrimeric complex with an iron-trisbipyridyl [Fe(Bpy-ala)3]2+ core when expressed in E. coli, its subsequent utility was marred by an excessively strong protein-protein interaction thus leading to a lack of metal-dependency. This thesis describes principles of protein design and characterization used to reduce the favorability of the apo protein complex in solution, resulting in the experimental verification of a mutant that undergoes facile, reversible complex assembly and disassembly in the presence or absence of Fe(II), respectively. The addition of other metal ions, such as Co(II) or Ni(II), yields products that show some level of assembly, although not with the same efficiency as Fe(II) addition, necessitating a better description of the energetics and kinetics of the system. Current studies are ongoing to examine the redox properties of the complex, as well as the kinetics of the metal-mediated self-assembly. Attempts to nucleate the trimer with Ru(II), forming a [Ru(Bpy)3]2+ complex with its interesting photophysical, photochemical, and photoredox properties, have not been met with substantial success, as coordination of the low-spin d6 metal ion often requires harsh conditions. However, due to the unique stability of the TRI_05 complexes, many approaches are available to this end, and experiments are underway to elucidate the proper conditions.
ContributorsAlmhjell, Patrick James (Author) / Mills, Jeremy H. (Thesis director) / Moore, Gary F. (Committee member) / Department of Psychology (Contributor) / School of Molecular Sciences (Contributor) / School of Life Sciences (Contributor) / Barrett, The Honors College (Contributor)
Created2017-05