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

The electrostatic properties of proteins arise from the number and distribution of polar and charged residues. Electrostatic interactions in proteins play a critical role in numerous processes such as molecular recognition, protein solubility, viscosity, and antibody developability. Thus, characteri...

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Veröffentlicht in:Journal of chemical information and modeling 2023-11, Vol.63 (22), p.6964-6971
Hauptverfasser: Hoerschinger, Valentin J, Waibl, Franz, Pomarici, Nancy D, Loeffler, Johannes R, Deane, Charlotte M, Georges, Guy, Kettenberger, Hubert, Fernández-Quintero, Monica L, Liedl, Klaus R
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Sprache:eng
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Zusammenfassung:The electrostatic properties of proteins arise from the number and distribution of polar and charged residues. 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 are prerequisites for understanding these processes. Here, we present PEP-Patch, a tool to visualize and quantify the electrostatic potential on the protein surface in terms of surface patches, denoting separated areas of the surface with a common physical property. We highlight its applicability to elucidate protease substrate specificity and antibody-antigen recognition and predict heparin column retention times of antibodies as an indicator of pharmacokinetics.
ISSN:1549-9596
1549-960X
1549-960X
DOI:10.1021/acs.jcim.3c01490