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Polymer- protein interface and high throughput screening for protein structural stability

Author(s): Vaishnavi Parikh

Role of polymers is substantial in delivering protein drugs. Delivery of proteins; however, is challenging due to complex interactions including hydrophobic interaction, electrostatic interaction, hydrogen bonding and interaction between adsorbed protein molecules which may lead to loss of protein stability. Several factors that affect these interactions include polymer type, surface charge, pH and ionic strength of the solvent system, presence of competing proteins. It is critical to attain mechanistic understanding of adsorption of proteins at solid/ liquid interfaces to deliver the protein in safe and effective form at the site of action. Use of different polymers intended for drug delivery and analytical techniques such as dynamic light scattering spectroscopy, fluorescence spectroscopy and circular dichroism spectroscopy is demonstrated to screen the factors for development of stable dosage form. Evaluation of the changes in secondary and tertiary structure of recombinant human growth hormone (r-hGH) upon adsorption at biodegradable Poly (lactideco- glycolide) PLGA nanoparticles of different hydrophobicity as a function of pH is illustrated to understand the nature of the interactions that govern the adsorption of the protein on the polymer, leading to successful design of sustained delivery systems.

This work is partly presented at 8th Edition of International Conference on Chemistry Education and Research August 27-28, 2018


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