Web-based display of protein surface and pH-dependent properties for assessing the developability of biotherapeutics.

ABSTRACT: Protein instability leads to reversible self-association and irreversible aggregation which is a major concern for developing new biopharmaceutical leads. Protein solution behaviour is dictated by the physicochemical properties of the protein and the solution. Optimising protein solutions through experimental screens and targeted protein engineering can be a difficult and time consuming process. Here, we describe development of the protein-sol web server, which was previously restricted to protein solubility prediction from amino acid sequence. Tools are presented for calculating and mapping patches of hydrophobicity and charge on the protein surface. In addition, predictions of folded state stability and net charge are displayed as a heatmap for a range of pH and ionic strength conditions

SUBMITTER: Hebditch M 

PROVIDER: S-EPMC6374528 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature