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Peptide and Protein Interaction with Membrane Systems: Applications to Antimicrobial Therapy and Protein Drug Delivery: Springer Theses

Autor Sara Bobone
en Limba Engleză Hardback – 24 iun 2014
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 nano devices described in this thesis could solve many of the hurdles still hampering the therapeutic application of protein-based drugs.
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Specificații

ISBN-13: 9783319064338
ISBN-10: 3319064339
Pagini: 140
Ilustrații: XIII, 140 p. 94 illus., 18 illus. in color.
Dimensiuni: 155 x 235 x 17 mm
Greutate: 0.4 kg
Ediția:2014
Editura: Springer International Publishing
Colecția Springer
Seria Springer Theses

Locul publicării:Cham, Switzerland

Public țintă

Research

Cuprins

Overview.- Antimicrobial Peptides: Mechanism of Action, Selectivity and Biological Activity.- Introduction.- Techniques.- Materials and Methods.- Results and Discussion.- Hydrogel Nanoparticles for Enzyme-Based Therapies.- Introduction.- Materials and Methods.- Results and Discussion.- Concluding Remarks.

Notă biografică

I received my M.Sc. Degree in Chemistry magna cum laude from the University of Rome "Sapienza". After the degree, I moved to Tor Vergata, where I won a fellowship for PhD students in Chemical Sciences, under the supervision of Prof. L. Stella. I defended my thesis in 2013 and then continued my work as a postdoctoral fellow. The thesis was awarded the 2012-2013 "Premio Semerano" by the Italian Chemical Society, as the best Italian PhD Physical Chemistry Thesis. The thesis work led to the publication of 7 papers on international journals and to the participation to 13 international and national conferences.

Textul de pe ultima copertă

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.

Caracteristici

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 Includes supplementary material: sn.pub/extras