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dc.contributor.authorRainsford, Philip Ben
dc.contributor.authorRylandsholm, Fredrik G.
dc.contributor.authorJakubec, Martin
dc.contributor.authorSilk, Mitchell
dc.contributor.authorJuskewitz, Eric
dc.contributor.authorEricson, Johanna Ulrica
dc.contributor.authorSvendsen, John Sigurd Mjøen
dc.contributor.authorEngh, Richard Alan
dc.contributor.authorIsaksson, Johan Mattias
dc.description.abstractOne strategy to combat antimicrobial resistance is the discovery of new classes of antibiotics. Most antibiotics will at some point interact with the bacterial membrane to either interfere with its integrity or to cross it. Reliable and efficient tools for determining the dissociation constant for membrane binding (K<sub><i>D</sub></i>) and the partitioning coefficient between the aqueous- and membrane phases (K<i><sub>P</i></sub>) are therefore important tools for discovering and optimizing antimicrobial hits. Here we demonstrate that microscale thermophoresis (MST) can be used for label-free measurement of K<i><sub>D</i></sub> by utilising the intrinsic fluorescence of tryptophan and thereby removing the need for chromophore labelling. As proof of principle, we have used the method to measure the binding of a set of small cyclic AMPs to large unilamellar vesicles (LUVs) and two types of lipid nanodiscs assembled by styrene maleic acid (SMA) and quaternary ammonium SMA (SMA-QA). The measured K<i><sub>D</i></sub> values correlate well with the corresponding measurements using surface plasmon resonance (SPR), also broadly reflecting the tested AMPs’ minimal inhibition concentration (MIC) towards S. aureus and E. coli. We conclude that MST is a promising method for fast and cost-efficient detection of peptide-lipid interactions or mapping of sample conditions in preparation for more advanced studies that rely on expensive sample preparation, labelling and/or instrument time.en_US
dc.identifier.citationRainsford, Rylandsholm, Jakubec, Silk, Juskewitz, Ericson, Svendsen, Engh, Isaksson. Label-free measurement of antimicrobial peptide interactions with lipid vesicles and nanodiscs using microscale thermophoresis. Scientific Reports. 2023en_US
dc.identifier.cristinIDFRIDAID 2228375
dc.publisherSpringer Natureen_US
dc.relation.journalScientific Reports
dc.rights.holderCopyright 2023 The Author(s)en_US
dc.rightsAttribution 4.0 International (CC BY 4.0)en_US
dc.titleLabel-free measurement of antimicrobial peptide interactions with lipid vesicles and nanodiscs using microscale thermophoresisen_US
dc.typeJournal articleen_US
dc.typePeer revieweden_US

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Attribution 4.0 International (CC BY 4.0)
Except where otherwise noted, this item's license is described as Attribution 4.0 International (CC BY 4.0)