One major challenge in producing protein therapeutics is their tendency to aggregate when stored at concentrations required for therapeutic efficacy. Here we demonstrate a novel in silico method for identifying aggregation-prone residues based on Poisson-Boltzmann hydrophobic patches and Accessible Surface Area (ASA) calculations. The method is fast, does not require computationally expensive molecular dynamics simulations, and can help identify (for mutation) critical residues that cause aggregation, but do affect specificity or efficacy.

Novel approach to detect and visualize aggregation-prone residues in immunoglobulins

245th National Meeting (2013)

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