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*Chilka R Patel, Dhara H Niranjani, Kirangi B Desai, P. K. Pradhan, U. M. Upadhyay

Department of Quality Assurance, Sigma Institute of Pharmacy, Vadodara, Gujarat, India.


Control and analysis of protein aggregation is an increasing challenge to pharmaceutical research and development. Due to the nature of protein interactions, protein aggregation may occur at various points throughout the lifetime of a protein and may be of different quantity and quality such as size, shape, morphology. It is therefore important to understand the interactions, causes and analyses of such aggregates in order to control protein aggregation to enable successful products. This review gives a short outline of currently discussed pathways and induction methods for protein aggregation and describes currently employed set of analytical techniques and emerging technologies for aggregate detection, characterization and quantification. A major challenge for the analysis of protein aggregates is that no single analytical method exists to cover the entire size range or type of aggregates which may appear. Each analytical method not only shows its specific advantages but also has its limitations. Size-exclusion chromatography (SEC) has been a workhorse for detecting and quantifying protein aggregation ([1,2]). But SEC is often questioned because of possible loss of proteins (soluble aggregates, in particular) by their nonspecific binding to the columns ([3]). Native gels have also been used to observe protein aggregation, but only qualitatively. Column-free techniques such as analytical ultracentrifugation (AUC), field-flow fractionation (FFF), and dynamic light scattering (DLS) now find increasing application in aggregation analysis.

Keywords: Aggregation, Electrophoresis, Size-Exclusion Chromatography,Analytical Ultracentrifugation, Dynamic Light Scattering, Field-Flow Fractionation.

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