Post-graduate theses
Current Record: 6 of 6124
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Identifier |
000454836 |
Title |
Self-assembly of aromatic-aliphatic dipeptides for controlled release applications |
Author
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Φανουράκη, Ειρήνη
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Thesis advisor
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Μητράκη, Άννα
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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.
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Language |
English |
Issue date |
2023-04-05 |
Collection
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School/Department--School of Medicine--Department of Medicine--Post-graduate theses
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Type of Work--Post-graduate theses
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Permanent Link |
https://elocus.lib.uoc.gr//dlib/c/9/d/metadata-dlib-1682676074-709071-3633.tkl
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Views |
6 |
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