Merli, Elisabetta (2010) Sintesi e indagine conformazionale preliminare di analoghi del peptide antimicrobico tilopeptina b contenenti come sonda EPR l' amminoacido TOAC. [Laurea specialistica biennale]
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Peptaibolics are a class of proteolitic enzyme-resistant, membrane active, linear, and cyclopeptides with antibiotic activity of fungal origin which may represent a useful scaffold for the construction of novel antibacterial drugs with promising properties. They are characterised by the presence of C alfa-tetrasubstituted alfa-amino acids alfa-amino-isobutyric acid (Aib). Linear peptaibolics have been classified in 3 classes according to the number of aminoacids in their sequence: long(17-21) , medium(14-16) and short(4-10). The mechanism of the second class is unknown. In this thesis we synthetized analogs of tylopeptin b, a medium peptaibolic (14 aminoacids), mono- and bis- labelled with TOAC electron spins . Labelled peptides, synthetised by solid phase synthesis (SPPS) technique with a new mild-condition approach, can be analysed by ESR spectroscopy, which can lead informations about its membranolitic mechanism activity. In this thesis preliminar conformational analysis is performed by circular dichroism and infrared spectroscopy which confirm that the helical-3D-structure is preferred in organic solvent and in the presence of anionic micelles, as the natural peptide tylopeptin b.
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