PEP-Patch: Electrostatics in Protein-Protein Recognition, Specificity and Antibody Developability

Waibl, F.; Pomarici, N. D.; Hoerschinger, V. J.; Loeffler, J. R.; Deane, C.; Georges, G.; Kettenberger, H.; Fernandez-Quintero, M. L.; Liedl, K. R.

doi:10.1101/2023.07.14.547811

bioRxiv · 10.1101/2023.07.14.547811

PEP-Patch: Electrostatics in Protein-Protein Recognition, Specificity and Antibody Developability

Waibl, F.·Pomarici, N. D.·Hoerschinger, V. J.·Loeffler, J. R.·Deane, C.·Georges, G.·Kettenberger, H.·Fernandez-Quintero, M. L.·Liedl, K. R.

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Abstract

The electrostatic properties of proteins arise from the number and distribution of polar and charged residues. Due to their long-ranged nature, electrostatic interactions in proteins play a critical role in numerous processes, such as molecular recognition, protein solubility, viscosity, and antibody developability. Thus, characterizing and quantifying electrostatic properties of a protein is a pre-requisite for understanding these processes. Here, we present PEP-Patch, a tool to visualize and quantify the electrostatic potential on the protein surface and showcase its applicability to elucidate protease substrate specificity, antibody-antigen recognition and predict heparin column retention times of antibodies as an indicator of pharmacokinetics.

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Waibl, F., Pomarici, N. D., Hoerschinger, V. J., Loeffler, J. R., Deane, C., Georges, G., Kettenberger, H., Fernandez-Quintero, M. L., Liedl, K. R.. 2023-07-15. PEP-Patch: Electrostatics in Protein-Protein Recognition, Specificity and Antibody Developability. https://doi.org/10.1101/2023.07.14.547811

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