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Nominated as an outstanding Ph.D. thesis by the University of Rome Tor Vergata, Italy
Selected as the as the best Italian Ph.D. Physical Chemistry Thesis 2012-2013 by the Italian Chemical Society
Provides a comprehensive but accessible introduction to both antimicrobial peptides and protein-based drugs: two hot areas in biomolecular pharmaceutics
Presents numerous examples of the use of fluorescence spectroscopy to characterize peptide and protein interaction with lipid membranes, which provide a good starting point for the novice in this field
In her thesis, Sara Bobone outlines spectroscopic studies of antimicrobial peptides (AMPs) which are promising lead compounds for drugs used to fight multidrug resistant bacteria. Bobone shows that AMPs interact with liposomes and she clarifies the structure of pores formed by one of these molecules. These results help us to understand how AMPs are selective for bacterial membranes and how their activity can be finely tuned by modifying their sequence. Findings which solve several conundrums debated in the literature for years. In addition, Bobone uses liposomes as nanotemplates for the photopolymerization of hydrogels - exploiting the self- assembly properties of phospholipids. Bobone was able to trap an enzyme using nanometeric particles, while still allowing its activity by the diffusion of substrates and products through the network of the polymer. The innovative nanodevices described in this thesis could solve many of the hurdles still hampering the therapeutic application of protein-based drugs.
Content Level »Research
Keywords »Enzyme Encapsulation - Fluorescence Spectroscopy - Mechanism of Action of Antimicrobial Peptides - Peptide-Membrane Interactions - Protein Drug Delivery - Selectivity of Antimicrobial Peptides