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dc.contributor.advisorBrandsdal, Bjørn Olav
dc.contributor.advisorIsaksen, Geir Villy
dc.contributor.authorBarge, Bente Sirin
dc.date.accessioned2020-04-29T08:41:35Z
dc.date.available2020-04-29T08:41:35Z
dc.date.issued2019-12-05
dc.description.abstractThe emerging crisis of antimicrobial resistance calls for the development of new therapeutic drugs. Antimicrobial peptides (AMPs), found in a variety of species as part of the host-defence mechanisms, serves as promising candidates for clinical use. Studies of well-known AMPs like lactoferrin have lead to the preparation of short cationic AMPs (CAPs) with broad spectrum antimicrobial activity against bacteria, fungi, enveloped viruses, parasites and cancer cells. However, in order for the CAPs to have therapeutic effect it must face and overcome several \textit{in vivo} challenges. One major hurdle is the proteolytic stability towards chymotrypsin, an enzyme present in the gastrointestinal tract. In this study, the interaction between chymotrypsin and active CAPs has been studied using molecular modelling and computer simulations. It was found that CAPs cleaved by the enzyme have stronger electrostatic interactions with the enzyme than the stable CAPs, both in the bound state and in the transition state. The stable CAPs were found to have structural features which can hinder optimal orientation of the main-chain in the transition state, and therefore lower the electrostatic stabilization. Furthermore, the enzyme was found to be preorganized with a polar environment that stabilizes the transition state more than the reactant state.en_US
dc.identifier.urihttps://hdl.handle.net/10037/18153
dc.language.isoengen_US
dc.publisherUiT Norges arktiske universiteten_US
dc.publisherUiT The Arctic University of Norwayen_US
dc.rights.accessRightsopenAccessen_US
dc.rights.holderCopyright 2019 The Author(s)
dc.rights.urihttps://creativecommons.org/licenses/by-nc-sa/4.0en_US
dc.rightsAttribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)en_US
dc.subject.courseIDKJE-3900
dc.subjectVDP::Matematikk og Naturvitenskap: 400::Kjemi: 440en_US
dc.subjectVDP::Mathematics and natural science: 400::Chemistry: 440en_US
dc.titleComputer Simulations of Antimicrobial Tripeptides with Proteolytic Stability Towards Chymotrypsinen_US
dc.typeMaster thesisen_US
dc.typeMastergradsoppgaveen_US


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Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
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