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Identifier 000454836
Title Self-assembly of aromatic-aliphatic dipeptides for controlled release applications
Author Φανουράκη, Ειρήνη
Thesis advisor Μητράκη, Άννα
Abstract Proteins and peptides are capable of spontaneously self-organizing into various structures such as fibrils, tubes, and ribbons. In the present dissertation the process of self-organization of dipeptide sequences composed of aromatic-aliphatic peptides in linear, circular, and protected forms was examined. More specifically, the peptides Phenylalanine-Leucine (FL), Leucine-Phenylalanine (LF), z-Phe-Phe, z-Phe-Leu, Fmoc-Phe-Phe, Boc-Phe-Phe, Fmoc-Phe- Leu and cyclo-Leu-Phe were studied and the dependence of the structures they form on factors such as concentration and effect of solvents. Z, (carboxybenzoxy), Fmoc (fluorenylmethoxy carbonyl), and Boc (tert-butyloxycarbonyl) are N-terminal protecting groups. The methods of experimental examination used in this research were FESEM electron microscopy and UV-Vis spectroscopy. The self-assembling propensity of the peptide drug Bortezomib (Pyz-Phe-boroLeu), which is a Phenylalanine-Leucine dipeptide protected at the Nterminus with a pyrazine moiety was studied, in its own form and in combination with the other dipeptides with the ultimate goal of exploring controlled release options for delivery. These peptides self-organized in a variety of ways, each with its own characteristics. The importance of peptide concentration, the ratio of “good” to “bad” solvent, and the peptide/drug ratio was also examined in this study.
Language English
Issue date 2023-04-05
Collection   School/Department--School of Medicine--Department of Medicine--Post-graduate theses
  Type of Work--Post-graduate theses
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