Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: 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.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2023
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
_version_ 1785151632010379264
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
work_keys_str_mv AT hoerschingervalentinj peppatchelectrostaticsinproteinproteinrecognitionspecificityandantibodydevelopability
AT waiblfranz peppatchelectrostaticsinproteinproteinrecognitionspecificityandantibodydevelopability
AT pomaricinancyd peppatchelectrostaticsinproteinproteinrecognitionspecificityandantibodydevelopability
AT loefflerjohannesr peppatchelectrostaticsinproteinproteinrecognitionspecificityandantibodydevelopability
AT deanecharlottem peppatchelectrostaticsinproteinproteinrecognitionspecificityandantibodydevelopability
AT georgesguy peppatchelectrostaticsinproteinproteinrecognitionspecificityandantibodydevelopability
AT kettenbergerhubert peppatchelectrostaticsinproteinproteinrecognitionspecificityandantibodydevelopability
AT fernandezquinteromonical peppatchelectrostaticsinproteinproteinrecognitionspecificityandantibodydevelopability
AT liedlklausr peppatchelectrostaticsinproteinproteinrecognitionspecificityandantibodydevelopability