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dc.contributor.advisorBrandsdal, Bjørn Olav
dc.contributor.authorSarre, Birta Ravdna
dc.date.accessioned2015-04-20T11:32:16Z
dc.date.available2015-04-20T11:32:16Z
dc.date.issued2014-12-17
dc.description.abstractSince the discovery of antibiotics the extensive use in health care and agriculture has led to the development of resistant bacterial strains. Antimicrobial peptides (AMPs) exists in nature where they are believed to play an important role in the innate immune system in vertebrates. Due to their antibacterial properties and apparent ability to elicit very low bacterial resistance, researchers have been hopeful that they can alleviate the challenges of progressing multiresistance, but this has not become a reality yet. In this project, molecular dynamics simulations are used to explore the interactions of AMPs with model lipid bilayers. An important step in this process is to obtain a lipid bilayer with structure and properties that resembles those of the biological relevant fluid phase (La) bilayer. By applying molecular dynamics it is possible to study the interaction at an atomic level. Atomic level studies of fluid phase (La) lipid bilayers are not possible with the present experimental methods. To examine the atomic level interactions of the synthetic antimicrobial peptides RWR-NHBn and RTbtR-NHBn with a bacterial like membrane, various DMPC and DMPG lipid bilayers are simulated with different combinations of the ions Na+, K+ and Cl-. Most combination of ions yield membrane properties in good agreement with experimental values. A binary mixture of DMPC/DMPG with K+ as counter-ions is used for the simulation with peptides. Interesting effects on the membrane is seen in a system with 4 TRTbtR-NHBn peptides where one peptide cause a large groove in the membrane surface by suppressing many DMPG lipids in the region. This may be a pre-stage to pore formation.en_US
dc.identifier.urihttps://hdl.handle.net/10037/7632
dc.identifier.urnURN:NBN:no-uit_munin_7221
dc.language.isoengen_US
dc.publisherUiT Norges arktiske universiteten_US
dc.publisherUiT The Arctic University of Norwayen_US
dc.rights.accessRightsopenAccess
dc.rights.holderCopyright 2014 The Author(s)
dc.subject.courseIDKJE-3900en_US
dc.subjectVDP::Mathematics and natural science: 400::Chemistry: 440::Theoretical chemistry, quantum chemistry: 444en_US
dc.subjectVDP::Matematikk og Naturvitenskap: 400::Kjemi: 440::Teoretisk kjemi, kvantekjemi: 444en_US
dc.titleMD simulations reveal how synthetic antimicrobial peptides interact with membrane modelsen_US
dc.typeMaster thesisen_US
dc.typeMastergradsoppgaveen_US


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