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PEP-Patch: Electrostatics in Protein–Protein Recognition, Specificity, and Antibody Developability
[Image: see text] 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...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2023
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10685443/ https://www.ncbi.nlm.nih.gov/pubmed/37934909 http://dx.doi.org/10.1021/acs.jcim.3c01490 |
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author | 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. |
author_facet | 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. |
author_sort | Hoerschinger, Valentin J. |
collection | PubMed |
description | [Image: see text] 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. |
format | Online Article Text |
id | pubmed-10685443 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-106854432023-11-30 PEP-Patch: Electrostatics in Protein–Protein Recognition, Specificity, and Antibody Developability 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. J Chem Inf Model [Image: see text] 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. American Chemical Society 2023-11-07 /pmc/articles/PMC10685443/ /pubmed/37934909 http://dx.doi.org/10.1021/acs.jcim.3c01490 Text en © 2023 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by/4.0/Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | 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. PEP-Patch: Electrostatics in Protein–Protein Recognition, Specificity, and Antibody Developability |
title | PEP-Patch: Electrostatics in Protein–Protein
Recognition, Specificity, and Antibody Developability |
title_full | PEP-Patch: Electrostatics in Protein–Protein
Recognition, Specificity, and Antibody Developability |
title_fullStr | PEP-Patch: Electrostatics in Protein–Protein
Recognition, Specificity, and Antibody Developability |
title_full_unstemmed | PEP-Patch: Electrostatics in Protein–Protein
Recognition, Specificity, and Antibody Developability |
title_short | PEP-Patch: Electrostatics in Protein–Protein
Recognition, Specificity, and Antibody Developability |
title_sort | pep-patch: electrostatics in protein–protein
recognition, specificity, and antibody developability |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10685443/ https://www.ncbi.nlm.nih.gov/pubmed/37934909 http://dx.doi.org/10.1021/acs.jcim.3c01490 |
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