Membrane interactions and biological activity of antimicrobial peptides from Australian scorpion |
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Authors: | Karen Luna-Ramí rez,Marc-Antoine Sani,Jesus Silva-Sanchez,Juana Marí a Jimé nez-Vargas,Fernando Reyna-Flores,Kenneth D. Winkel,Christine E. Wright,Lourival D. Possani,Frances Separovic |
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Affiliation: | 1. Australian Venom Research Unit, Department of Pharmacology, University of Melbourne, Victoria 3010, Australia;2. Cardiovascular Therapeutics Unit, Department of Pharmacology, University of Melbourne, Victoria 3010, Australia;3. School of Chemistry, Bio21 Institute, University of Melbourne, Melbourne, VIC 3010, Australia;4. Instituto Nacional de Salud Pública, Centro de Investigación sobre Enfermedades Infecciosas, Avenida Universidad 655, Cuernavaca, Morelos 62508, Mexico;5. Departamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Avenida Universidad, 2001, Colonia Chamilpa, Apartado Postal 510-3, Cuernavaca 62210, Mexico |
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Abstract: | UyCT peptides are antimicrobial peptides isolated from the venom of the Australian scorpion. The activity of the UyCT peptides against Gram positive and Gram negative bacteria and red blood cells was determined. The membrane interactions of these peptides were evaluated by dye release (DR) of the fluorophore calcein from liposomes and isothermal titration calorimetry (ITC); and their secondary structure was determined by circular dichroism (CD). Three different lipid systems were used to mimic red blood cells, Escherichia coli and Staphylococcus aureus membranes. UyCT peptides exhibited broad spectrum antimicrobial activity with low MIC for S. aureus and multi-drug resistant Gram negative strains. Peptide combinations showed some synergy enhancing their potency but not hemolytic activity. The UyCT peptides adopted a helical structure in lipid environments and DR results confirmed that the mechanism of action is by disrupting the membrane. ITC data indicated that UyCT peptides preferred prokaryotic rather than eukaryotic membranes. The overall results suggest that UyCT peptides could be pharmaceutical leads for the treatment of Gram negative multiresistant bacterial infections, especially against Acinetobacter baumanni, and candidates for peptidomimetics to enhance their potency and minimize hemolysis. This article is part of a Special Issue entitled: Interfacially Active Peptides and Proteins. Guest Editors: William C. Wimley and Kalina Hristova. |
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Keywords: | AMP, antimicrobial peptides Chol, cholesterol CD, circular dichroism DR, dye release ITC, isothermal titration calorimetry LPC, lipopolysaccharide LUV, large unilamellar vesicles MDR, multi-drug resistant MIC, minimum inhibitory concentration MRE, mean-residue ellipticity POPC, palmitoyloleoyl-phosphatidylcholine POPE, palmitoyloleoyl-phosphatidylethanolamine POPG, palmitoyloleoyl-phosphatidylglycerol RBC, red blood cell TOCL, tetraoeloyl-cardiolipin |
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