Stickiness:
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Understand surface activity of your samples
Assessment of sample stickiness provides valuable information about the surface activity of the sample. It can be used as a main readout, or as an embedded side-control metric to increase awarness about surface-sample interaction. The stickiness readout (taken as a side-metric in every assay) is a critical feature because, in many other technologies, the impact of sample stickiness is often overlooked, potentially leading to inaccurate or misleading results.
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Why measure sample stickiness?
Reducing False Positives Binding Assays in Drug Development and Discovery:
In some technologies, stickiness can lead to misleading results in binding assays, where non-specific interactions skew data. FIDA’s ability to detect stickiness in early stages helps researchers eliminate compounds prone to these interactions, improving the accuracy of binding assays.
Formulation - Stickiness management as a means for Optimizing Stability and Reducing Aggregation:
Stickiness in drug formulations, whether for biologics or small molecules, can cause unwanted aggregation or precipitation. But not in FIDA assays. FIDA’s stickiness measurement enables formulation scientists to adjust buffers, pH, or excipients to minimize non-specific interactions. This improves the stability of the formulation, reducing the need for costly reformulations and ensuring the drug remains effective over its shelf life.
Biologics - Improving Purity and Reducing Immunogenicity Risk:
For biologics, non-specific interactions can affect purity and lead to aggregation, increasing the risk of immunogenicity. FIDA’s stickiness measurement helps detect these interactions early, allowing for refinement of purification and formulation strategies. This boosts efficiency by preventing the need for later-stage fixes, ensuring that biologics maintain high purity and safety profiles.
Small Molecules: Enhancing Solubility and Delivery:
Small molecule drugs can exhibit stickiness that affects solubility and delivery, particularly in complex formulations. FIDA detects these non-specific interactions, enabling optimization of the solution environment to ensure the small molecule remains soluble and bioavailable. This reduces formulation failures and helps bring stable small molecule therapies to market faster.
Structural Biology: Improving Protein Model Accuracy:
In structural biology, non-specific stickiness can distort experimental results, leading to incorrect structural models. FIDA’s precise stickiness measurement allows researchers to identify and control these interactions, improving the accuracy of protein structure determination. This accelerates the validation of structural models and reduces the need for repeated experiments, speeding up the process of understanding protein functions and interactions.
FAQs
Would you like to know more? See frequently asked questions below. If you do not find an answer to your question, you can ask a question to one of our scientists.
Stickiness is an unspecific interaction between the protein/proteins with surfaces. The stickiness of biomolecules is influenced by various factors, including the presence of specific binding sites, electrostatic interactions, van der Waals forces, and hydrophobic interactions. Knowing the stickiness of your sample gives you the chance to be fully aware about interactions between your protein and different materials that will lead to downstream errors and misinterpretations of your data.
FIDA’s Rh measurement can detect molecular stickiness. Sticky molecules may affect the raw data outside the region of interest for measuring Rh. The asymmetry in the data is a sensitive measure of surface stickiness.
Yes, Fida Software can indicate if the sample is sticking to the capillary walls. It can also indicate whether the issue is fixed after assay optimisation.
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