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Tesi etd-09252016-194013


Thesis type
Tesi di laurea magistrale
Author
BONACCORSI, MARTA
URN
etd-09252016-194013
Title
Solid State NMR study of the interactions between a synthetic antimicrobial peptide and model cell membranes
Struttura
CHIMICA E CHIMICA INDUSTRIALE
Corso di studi
CHIMICA
Commissione
relatore Prof. Geppi, Marco
correlatore Prof. Cicero, Daniel Oscar
controrelatore Dott. Bernazzani, Luca
Parole chiave
  • solid state NMR
  • antimicrobial peptide
  • membrane
Data inizio appello
20/10/2016;
Consultabilità
parziale
Data di rilascio
20/10/2019
Riassunto analitico
This thesis work concerns the study of the interactions between the synthetic antimicrobial peptide (YI13C)2 and model cell membranes by Solid State Nuclear Magnetic Resonance (SSNMR) techniques. <br>The strategy used for the study involved the preparation of POPC ( 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine) model cell membranes and the application of a multi-nuclear and multi-technique solid state NMR approach to study the interactions between the components of the system at a molecular level. Both non aligned and mechanically aligned samples were prepared and studied. The observation of the nuclei 31P, 2H, 1H and the measurement of different spectral properties gave structural and dynamic information on both the polar region of the bilayers and the water contained in the phase. <br>From the study of non aligned samples a perturbative effect of the peptide on the bilayer structure and on the dynamic properties of water molecules was shown. The dependence of the perturbation on the concentration of the peptide and on the hydration of the membranes was revealed. The exploitation of mechanical alignment gave further information on the perturbation mechanism.<br>From a compared analysis of all the experimental results some hints on the model of action of the peptide in the system studied were obtained. <br>In addition, the properties of differently purified samples of LPS (lipopolysaccharide) in aqueous environment were preliminarily studied by 31P SSNMR.
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