Homogenization of the bulk LLC forms dispersions of particles, ∼200 nm in diameter with internal bicontinuous primitive cubic phases, as seen using small-angle X-ray scattering and cryo-transmission electron microscopy. Azobenzene photosurfactants (AzoPS), containing a neutral tetraethylene glycol head group and azobenzene-alkyl tail, are combined (from 10–30 wt %) into monoolein-water systems to create LLC phases. In this work, we demonstrate the first example of light-responsive cubic LLC dispersions, or cubosomes, using photoswitchable amphiphiles to enable external control over the LLC structure and subsequent on-demand release of entrapped guest molecules. Lyotropic liquid crystals (LLCs) have well-defined internal structures suitable to entrap small molecules and can be broken up into low-viscosity dispersions, aiding their application as delivery systems. If you think DLS could be a valuable tool for your research, or you are interested in learning more about the details of how it works to give us particle sizing information, watch this short informational webinar about DLS.Stimuli-responsive materials are crucial to advance controlled delivery systems for drugs and catalysts. Any researcher looking for deep biophysical understanding of their favorite protein can benefit from the information provided by DLS. The ability to monitor how buffers, additives, and substrates can help drive better understanding of mechanisms and stability. Self-interaction can be measured with DLS, giving researchers the K d of their protein of interest.ĭLS is a powerful tool for characterizing your protein. The ability to monitor this process in vitro can help researchers to develop assays that allow them to better understand how the changes in protein-self interaction triggers other responses. Oligomerization affects protein activityĬell biologists know the importance of oligomerization in cellular processes. Subtle changes in the r h can be screened to determine binders.Ĥ. But binding often introduces a change in the structure of the protein, which can expand or contract to bind small molecules. No method is 100% reliable in avoiding either false positives or false negatives. Binding events affect a protein’s sizeĭrug developers looking for the next big breakthrough often have huge libraries of compounds to screen. Having a better picture of how this affects your protein’s size and polydispersity allows researchers to make better decisions about what constructs to move forward with in the lab.ģ. Each mutation offers the potential to alter protein behaviour for better or worse. By editing the sequence of a protein or antibody, researchers can create a biological molecule with increased substrate affinity, better long-term storage stability, or additional binding sites. Protein engineering is a key element in optimizing proteins for everything from benchtop assays to therapeutics in the clinic. If a buffer has a negative impact on protein stability, this will be reflected in the broadening of that peak and an increase in PDI. Proteins that are tightly folded and stable give a single, sharp peak at the r h when looking at the size distribution. Anyone who has worked in biologics formulation knows that storage and assay buffers alike must be optimized to ensure a protein remains stable and functional for a long time. Researchers almost exclusively work with proteins in buffer. Why is it useful to have particle sizing information? It can also determine if there are multiple particle sizes present in the sample by determining the polydispersity index (PDI). This information can be correlated to the hydrodynamic radius (r h) of the particle that scattered the light. The DLS instrument then collects how intense or bright that scattered light is at a fixed angle. It works by sending a monochromatic beam of light into your sample the sample bounces, or scatters, that light in different directions. Here’s an overview of DLS and how it’s useful for your protein research.ĭynamic Light Scattering, or DLS, is a technique that gives you detailed information about the size of your biological particles. Any researcher looking to better understand their protein’s behavior can benefit from the information provided by Dynamic Light Scattering (DLS).
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