Antimicrobial Action of the Cyclic Peptide Bactenecin on Burkholderia pseudomallei Correlates with Efficient Membrane Permeabilization.docVIP

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Antimicrobial Action of the Cyclic Peptide Bactenecin on Burkholderia pseudomallei Correlates with Efficient Membrane Permeabilization.doc

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Antimicrobial Action of the Cyclic Peptide Bactenecin on Burkholderia pseudomallei Correlates with Efficient Membrane Permeabilization

AntimicrobialActionoftheCyclicPeptideBactenecinon BurkholderiapseudomalleiCorrelateswithEfficient MembranePermeabilization KanjanaMadhongsa1,2,SupalukPasan1,2,OnanongPhophetleb1,2,SawineeNasompag1,2 SompongThammasirirak1,2,SakdaDaduang1,2,SuwimolTaweechaisupapong3,4,AndreiL.Lomize5, RinaPatramanon1,2¤ , * 1ProteinandProteomicsResearchCenterforCommercialandIndustrialPurposes(ProCCI),KhonKaenUniversity,KhonKaen,Thailand,2DepartmentofBiochemistry, Faculty of Science, Khon Kaen University, Khon Kaen, Thailand, 3Melioidosis Research Center, Khon Kaen University, Khon Kaen, Thailand, 4Biofilm Research Group, FacultyofDentistry,KhonKaenUniversity,KhonKaen,Thailand,5CollegeofPharmacy,UniversityofMichigan,AnnArbor,Michigan,UnitedStatesofAmerica Abstract BurkholderiapseudomalleiisacategoryBagentthatcausesMelioidosis,anacuteandchronicdiseasewithsepticemia.The currenttreatmentregimenisaheavydoseofantibioticssuchasceftazidime(CAZ);however,theriskofarelapseispossible. Peptide antibiotics are an alternative to classical antibiotics as they exhibit rapid action and are less likely to result in the developmentofresistance.TheaimofthisstudywastodeterminethebactericidalactivityagainstB.pseudomalleiandexamine themembranedisruptingabilitiesofthepotentantimicrobialpeptides:bactenecin,RTA3,BMAP-18andCA-MA.Allpeptides exhibited .97% bactericidal activity at 20mM, with bactenecin having slightly higher activity. Long term time-kill assays revealed a complete inhibition of cell growth at 50mM bactenecin and CA-MA. All peptides inhibited biofilm formation comparable to CAZ, but exhibited faster kinetics (within 1h). Bactenecin exhibited stronger binding to LPS and induced perturbationofthe inner membrane of live cells. Interactionofbactenecin with model membranes resulted in changes in membranefluidityandpermeability,leadingtoleakageofdyeacrossthemembraneatlevelstwo-foldgreaterthanthatofother peptides.Modelingofpeptidebindingonthemembraneshowedstableanddeepinsertionofbactenecinintothemembran