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Please use this identifier to cite or link to this item: http://hdl.handle.net/2108/218

Title: Il meccanismo di azione del peptide antibiotico Tricogina GA IV: studi chimico-fisici su analoghi fluorescenti
Authors: Crociani, Bruno
Mazzuca, Claudia
Keywords: Trichogin GA IV
peptide-membrane interactions
fluorescence spectroscopy
fluorescence spectroscopy
Issue Date: 6-Mar-2006
Abstract: “Mechanism of membrane perturbation by the antibiotic peptide Trichogin GAIV: a physico-chemical study on fluorescent analogs” dr. Claudia Mazzuca Trichogin GA IV is the main component of the lipopeptaibol family, an important class of antibiotic linear peptides, which exert their action by perturbing the permeability of cell membranes, without interacting with any specific receptor. Trichogin sequence is characterized by an N-terminal fatty acyl group, a C-terminal 1,2-amino alcohol and a high proportion of Aib residues: Oct-Aib-Gly-Leu-Aib-Gly-Gly-Leu-Aib-Gly-Ile-Lol where Oct is n-octanoyl and Lol is leucinol. This peptide displays a remarkable antibacterial and hemolytic activity, but the details of its mode of action are still unsettled. In order to characterize the behavior of trichogin, we decided to take advantage of the high sensibility of fluorescence spectroscopy: therefore, two trichogin analogues marked with fluorescent probes (fluorene and azulene) were synthesiz...
URI: http://hdl.handle.net/2108/218
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