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Comprehensive protein stabilizing screening study included conformational analysis of formulated rHuG-CSF protein to obtain information on its secondary structure conformational stability.
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As a basis a new selection strategy that allowed the application of yeast surface display for screening of stabilizing mutations in proteins of already high intrinsic thermal stability and Tm-values up to 85 °C was developed.
To enhance the physical stability of Clostridium difficile toxoids A and B, screening for stabilizing compounds was performed.
That is why screening of stabilizing agent(s) is important in developing a formulation containing a highly soluble cocrystal of poorly water soluble APIs.
The aim of this work was to advance yeast surface display for screening of stabilizing point mutations in proteins that have already a high intrinsic conformational and thermal stability.
Various classes of pharmaceutical excipients were screened for their stabilizing effect on dmLT during exposure to thermal and agitation stresses as monitored by high throughput analytical assays for dmLT degradation.
Based on the screening studies four representative stabilizing ligands were chosen for further investigations.
Optimum parameters of dispersion stabilizing were identified in a systematic screening based on zeta potential measurements.
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Screening DSII via DSF revealed a number of stabilizing ligands, which were in turn treated as active compounds for the virtual screen.
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