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In the present study, we have investigated the behaviour of anandamide in various membrane environments with or without cholesterol, using both monolayer and bilayer membrane models systems.
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Reyes, L. F. et al. The role of the C-terminal region of pulchellin A-chain in the interaction with membrane model systems.
The present study is a first step towards the investigation of S-methyl methanethiosulfonate (MMTS) interaction with membrane model systems like liposomes.
Fluorescence microscopy studies using giant unilamellar vesicles (GUVs) as membrane model systems provide a unique methodology to quantify protein binding, interaction, and lipid solubilization in artificial bilayers.
In the last few years it has become clear that the behavior of antimicrobial peptides on membrane model systems does not always translate to cells; therefore the need to develop methods aimed at capturing details of the interactions of peptides with bacterial cells is compelling.
Previous studies established the relative preferences of these peptides for membrane model systems of defined lipid compositions.
Figure S3 KTP-NH2 interaction with membrane model systems.
Several studies have reported the mechanisms of pulchellin interaction with membrane model systems [ 4] and the endocytosis machinery in K-562 cells [ 2], but there have been no reports of the immunological activities of this protein.
Our preliminary data regarding KTP-NH2 interaction with membrane model systems indicates a preference of this molecule for fluid, negatively charged, membranes, which indicates different profiles of interaction for these two compounds (morphine and KTP-NH2)and supports the hypothesis of distinct molecular modes of action.
Data acquisition with this lipid membrane model system is highly re-producible.
This process has recently been reconstituted with an inside-out membrane model system using giant unilamellar vesicles providing a compelling explanation of how FGF2 reaches the extracellular space in an ER/Golgi independent manner.
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