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Effects of Antimicrobial Peptide Revealed by Simulations Translocation, Pore Formation, Membrane Corrugation and Euler Buckling.doc

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Effects of Antimicrobial Peptide Revealed by Simulations Translocation, Pore Formation, Membrane Corrugation and Euler Buckling

Int.J.Mol.Sci.2013,14,7932-7958;doi:10.3390/ijmOPENACCESS InternationalJournalof MolecularSciences ISSN1422-0067 /journal/ijms Article EffectsofAntimicrobialPeptideRevealedbySimulations: Translocation,PoreFormation,MembraneCorrugationand EulerBuckling LicuiChen ,NanaJia * 1 1,LianghuiGao 1,*,WeihaiFang 1andLeonardoGolubovic 2, 1 KeyLaboratoryofTheoreticalandComputationalPhotochemistry,MinistryofEducation, CollegeofChemistry,BeijingNormalUniversity,Beijing100875,China; E-Mails: chenlicui@163.com(L.C.);jiananaok@(N.J.);fangwh@(W.F.) PhysicsDepartment,WestVirginiaUniversity,Morgantown,WV26506-6315,USA 2 *Authorstowhomcorrespondenceshouldbeaddressed;E-Mails:lhgao@(L.Ga.); lgolubov@(L.Go.);Tel.:+86-10-5880-2003(L.Ga.);+1-304-293-5195(L.Go.); Fax:+86-10-5880-2003(L.Ga.);+1-304-293-5732(L.Go.). Received:9January2013;inrevisedform:5March2013/Accepted:27March2013/ Published:11April2013 Abstract: We explore the effects of the peripheral and transmembrane antimicrobial peptides on the lipid bilayer membrane by using the coarse grained Dissipative Particle Dynamicssimulations.Westudypeptide/lipidmembranecomplexesbyconsideringpeptides with various structure, hydrophobicity and peptide/lipid interaction strength. The role of lipid/water interaction is also discussed. We discuss a rich variety of membrane morphologicalchangesinducedbypeptides,suchasporeformation,membranecorrugation andEulerbuckling. Keywords:antimicrobialpeptides;membrane;dissipativeparticledynamics 1.Introduction Antimicrobial peptides (AmPs) are one kind of membrane-lytic peptides that serve as defense weaponsagainstbacteria[1].TheAmPsaresecretedbyorganismsofplantsandanimalsandhaveawide varietyincompositionandstructure[2,3]. Theseshortchainpeptidesareusuallycomposedof12–45 aminoacidresiduesthatcarrypositivecharges. Whenbindingontotheoutermostlea?etofnegatively Int.J.Mol.Sci.2013,14 7933 chargedbacteriamembranesbytheaidofhydrophobic