Browsing by Author "Darkwah, Joseph"
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Characterisation of freeze dried amino acids and gelatin based rapidly Disintegrating tablets
Darkwah, Joseph (Thesis or dissertation / Masters / MPhil)Recent research has shown the feasibility of using individual or a combination of amino acids as a replacement component for sugars in RDT formulations. What has emerged from this work is the notion of an optimal concentration ... -
Effect of acidic and basic pH on Thioflavin T absorbance and fluorescence
Hackl, E. V.; Darkwah, Joseph; Smith, Geoff; Ermolina, I. (Article)Thioflavin T (ThT) is a fluorescent dye able to enhance significantly its fluorescence quantum yield upon binding to protein amyloids. ThT assay is widely used to detect and quantify amyloids in a variety of conditions, ... -
Effect of arginine on the aggregation of protein in freeze-dried formulations containing sugars and polyol. 1. Formulation development
Hackl, E. V.; Darkwah, Joseph; Smith, Geoff; Ermolina, I. (Article)L-arginine was introduced into protein-based freeze-dried formulations to study the ability of arginine to reduce / prevent from protein aggregation during manufacturing, storage and reconstitution of lyophilized protein-based ... -
Effect of Arginine on the Aggregation of Protein in Freeze-Dried Formulations Containing Sugars and Polyol: II. BSA Reconstitution and Aggregation
Hackl, E. V.; Darkwah, Joseph; Smith, Geoff; Ermolina, I. (Article)The current paper continues our study on the ability of L-arginine to prevent/reduce the aggregation of proteins that results from the various stresses during the lyophilisation and/or storage of lyophilized protein-based ... -
Protein stability: Impact of formulation excipients and manufacturing processes in protein-based pharmaceuticals
Darkwah, Joseph (Thesis or dissertation / Doctoral / PhD)Presently, over 300 proteins or peptide based therapeutic medicines have been approved by the FDA owing to advances in protein engineering and technology. However, majority of these protein-based medications are unstable ...