Limatola, Antonio (2015) NMR spectroscopy: a useful tool for drugs development and monitoring biological reactions. [Tesi di dottorato]


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Tipologia del documento: Tesi di dottorato
Lingua: English
Titolo: NMR spectroscopy: a useful tool for drugs development and monitoring biological reactions
Data: 31 Marzo 2015
Numero di pagine: 137
Istituzione: Università degli Studi di Napoli Federico II
Dipartimento: Farmacia
Scuola di dottorato: Scienze farmaceutiche
Dottorato: Scienza del farmaco
Ciclo di dottorato: 27
Coordinatore del Corso di dottorato:
D'Auria, Maria
Carotenuto, Alfonso[non definito]
Data: 31 Marzo 2015
Numero di pagine: 137
Parole chiave: NMR spectroscopy; conformational analysis; drug development; in-cell NMR
Settori scientifico-disciplinari del MIUR: Area 05 - Scienze biologiche > BIO/10 - Biochimica
Area 05 - Scienze biologiche > BIO/11 - Biologia molecolare
Area 03 - Scienze chimiche > CHIM/02 - Chimica fisica
Area 03 - Scienze chimiche > CHIM/08 - Chimica farmaceutica
Depositato il: 10 Apr 2015 11:52
Ultima modifica: 28 Apr 2018 01:00
DOI: 10.6093/UNINA/FEDOA/10433


Background of my doctoral PhD program is primarily based on the use of nuclear magnetic resonance spectroscopy (NMR) as a versatile tool that can be applied for several biological purposes. During the early years of my PhD, I mainly used proton detection nuclear magnetic resonance techniques (1H-NMR) for the identification and characterization of molecules that can act as potential drugs. Since, GPCRs are targeted by approximately 45% to 50% of medicinal drugs, I focused my attention on the development and conformational analysis of peptides modulating a few of these receptors bringing to different therapeutic effects. During the last period of my PhD, I used NMR spectroscopy techniques based on 15N and/or 13C detection. Techniques suitable to study much larger systems as whole proteins. I applied in-cell, in extracts and in vitro NMR spectroscopy techniques to study and monitor in a qualitative and quantitative manner biological reactions that can occur on a protein into a biological environment. In particular, I studied the intracellular fate of oxidized α‑synucein molecules.

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