Martino, Luigi (2009) DNA QUADRUPLEXES AND PROTEINS: STRUCTURE, STABILITY AND THEIR INTERACTIONS WITH PHARMACOLOGICALLY RELEVANT MOLECULES. [Tesi di dottorato] (Inedito)

[img] PDF
Martino.pdf
Visibile a [TBR] Amministratori dell'archivio

Download (16MB)
Tipologia del documento: Tesi di dottorato
Lingua: English
Titolo: DNA QUADRUPLEXES AND PROTEINS: STRUCTURE, STABILITY AND THEIR INTERACTIONS WITH PHARMACOLOGICALLY RELEVANT MOLECULES
Autori:
AutoreEmail
Martino, Luigiluigi.martino@unina.it
Data: 25 Novembre 2009
Numero di pagine: 97
Istituzione: Università degli Studi di Napoli Federico II
Dipartimento: Chimica "Paolo Corradini"
Scuola di dottorato: Scienze chimiche
Dottorato: Scienze chimiche
Ciclo di dottorato: 22
Coordinatore del Corso di dottorato:
nomeemail
Vitagliano, Aldoalvitagl@unina.it
Tutor:
nomeemail
Giancola, Concettaconcetta.giancola@unina.it
Data: 25 Novembre 2009
Numero di pagine: 97
Parole chiave: Quadruplex Structures, NMR, ITC, CD, isomerase,
Settori scientifico-disciplinari del MIUR: Area 03 - Scienze chimiche > CHIM/02 - Chimica fisica
Informazioni aggiuntive: Indirizzo del dottorato: Riconoscimento molecolare in processi di interesse biologico ed ambientale
Depositato il: 03 Ago 2010 14:39
Ultima modifica: 29 Ott 2014 12:17
URI: http://www.fedoa.unina.it/id/eprint/4066

Abstract

In the first part of the thesis my efforts have been focused on the interactions between the DNA quadruplex structures and drugs such as distamycin A and cationic porphyrin. Those drug are able to bind to the quadruplex structure via to completely different binding mode. The distamycin A is a well-know groove binder on the other hand the cationic porphyrin prefers stacking-mode interacting mechanisms. For the previous reasons those molecules are a good starting point, as molecular scaffold, for further chemical optimisations that could enhance their affinity for the quadruplex structures. In a second stage of my PhD studies, I had the possibility to move to the lab of Dr. Maria R Conte at the King’s College of London to further my understanding of protein NMR. In this stimulating environment I started to study the structure and the interaction of the protein SlyD from E.coli. This system represented the possibility to apply all my biophysical skills to the field of the proteins. In my thesis work I faced the study of three different systems, with increasing complexity. All the interactions, that have been characterised, are biological relevant and the study intends to illuminate on their structural and energetic aspects in order to get a deeper understanding of their regulating mechanisms.

Actions (login required)

Modifica documento Modifica documento