MIHAELA BACALUM*, HELGE WEINGART**, M. RADU*
*Department of Life and Environmental Physics, “Horia Hulubei” National Institute for Physics and Nuclear Engineering, PO Box MG6, Măgurele, 077125, Romania, firstname.lastname@example.org
**School of Engineering and Science, Jacobs University Bremen, Bremen, 28759, Germany
Abstract. Porins found in the outer membrane of Gram negative bacteria are considered to be one of the pathways used by antibiotics to cross the membrane. However, in time, bacteria have developed different mechanisms to fight the antibiotics and preventing them to reach the target. Studying the interaction between outer membrane porin F (OmpF) and antibiotics will help understand better these mechanisms. The insertion the OmpF (extracted form Escherichia coli) into homogeneous and heterogeneous liposomes membranes was studied by fluorescence resonance energy transfer (FRET) technique. The quenching of OmpF tryptophane residues fluorescence by ceftazidime (a β-lactam family antibiotic) allowed describing the interaction between the antibiotic and the porin.
Key words: antibiotics, FRET, liposomes, OmpF, protein insertion.
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