Abate, Luigi
(2020)
Design, synthesis and biological activity of peptides and peptidomimetics as modulators the urotensinergic system.
[Tesi di dottorato]
| Tipologia del documento: |
Tesi di dottorato
|
| Lingua: |
English |
| Titolo: |
Design, synthesis and biological activity of peptides and peptidomimetics as modulators the urotensinergic system |
| Autori: |
| Autore | Email |
|---|
| Abate, Luigi | luigi.abate@unina.it |
|
| Data: |
12 Marzo 2020 |
| Numero di pagine: |
114 |
| Istituzione: |
Università degli Studi di Napoli Federico II |
| Dipartimento: |
Farmacia |
| Dottorato: |
Scienza del farmaco |
| Ciclo di dottorato: |
32 |
| Coordinatore del Corso di dottorato: |
| nome | email |
|---|
| D'Auria, Valeria | [non definito] |
|
| Tutor: |
| nome | email |
|---|
| grieco, Paolo | [non definito] |
|
| Data: |
12 Marzo 2020 |
| Numero di pagine: |
114 |
| Parole chiave: |
Peptide synthesis, Urotensin-II, Biological data |
| Settori scientifico-disciplinari del MIUR: |
Area 03 - Scienze chimiche > CHIM/08 - Chimica farmaceutica |
[error in script]
[error in script]
| Depositato il: |
19 Mar 2020 11:37 |
| Ultima modifica: |
08 Nov 2021 12:31 |
| URI: |
http://www.fedoa.unina.it/id/eprint/13121 |
Abstract
In the humane, the urotensinergical system is involved in several pathological conditions, from cardiovascular disease at the neoplastic condition. The urotensinergical system is mediated by two cyclic peptides U-II and URP, these conserve the same cyclic region but differ the N-terminal domain. Previous studies have individuated two lead compounds P5U and Urantide, respectively superagonist and antagonist for the UT receptor. To improve the antagonistic activity of Urantide, the research activity of my PhD has been focused on Design, synthesis and characterization of analogues of this peptide. In particular, I’ve performed the synthesis of three different libraries of compounds that they have characterized the introduction of analogues of Tyrosine, Lysine, in respective position and the modification of the N-terminal domain. Another goal has been characterized at structural studies of URP through the use of peptoids and N-methylation, to better define the structural elements that allow maintaining the peptide bioactive structure. These modifications have been carried out to improve the knowledge of elements that improve the antagonistic activity so that these peptides could be used at the therapeutic scope.
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