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RASPD+: Fast Protein-Ligand Binding Free Energy Prediction Using Simplified Physicochemical Features

The virtual screening of large numbers of compounds against target protein binding sites has become an integral component of drug discovery workflows. This screening is often done by computationally docking ligands into a protein binding site of interest, but this has the drawback of a large number...

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Autores principales: Holderbach, Stefan, Adam, Lukas, Jayaram, B., Wade, Rebecca C., Mukherjee, Goutam
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7773945/
https://www.ncbi.nlm.nih.gov/pubmed/33392260
http://dx.doi.org/10.3389/fmolb.2020.601065
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author Holderbach, Stefan
Adam, Lukas
Jayaram, B.
Wade, Rebecca C.
Mukherjee, Goutam
author_facet Holderbach, Stefan
Adam, Lukas
Jayaram, B.
Wade, Rebecca C.
Mukherjee, Goutam
author_sort Holderbach, Stefan
collection PubMed
description The virtual screening of large numbers of compounds against target protein binding sites has become an integral component of drug discovery workflows. This screening is often done by computationally docking ligands into a protein binding site of interest, but this has the drawback of a large number of poses that must be evaluated to obtain accurate estimates of protein-ligand binding affinity. We here introduce a fast pre-filtering method for ligand prioritization that is based on a set of machine learning models and uses simple pose-invariant physicochemical descriptors of the ligands and the protein binding pocket. Our method, Rapid Screening with Physicochemical Descriptors + machine learning (RASPD+), is trained on PDBbind data and achieves a regression performance that is better than that of the original RASPD method and traditional scoring functions on a range of different test sets without the need for generating ligand poses. Additionally, we use RASPD+ to identify molecular features important for binding affinity and assess the ability of RASPD+ to enrich active molecules from decoys.
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spelling pubmed-77739452021-01-01 RASPD+: Fast Protein-Ligand Binding Free Energy Prediction Using Simplified Physicochemical Features Holderbach, Stefan Adam, Lukas Jayaram, B. Wade, Rebecca C. Mukherjee, Goutam Front Mol Biosci Molecular Biosciences The virtual screening of large numbers of compounds against target protein binding sites has become an integral component of drug discovery workflows. This screening is often done by computationally docking ligands into a protein binding site of interest, but this has the drawback of a large number of poses that must be evaluated to obtain accurate estimates of protein-ligand binding affinity. We here introduce a fast pre-filtering method for ligand prioritization that is based on a set of machine learning models and uses simple pose-invariant physicochemical descriptors of the ligands and the protein binding pocket. Our method, Rapid Screening with Physicochemical Descriptors + machine learning (RASPD+), is trained on PDBbind data and achieves a regression performance that is better than that of the original RASPD method and traditional scoring functions on a range of different test sets without the need for generating ligand poses. Additionally, we use RASPD+ to identify molecular features important for binding affinity and assess the ability of RASPD+ to enrich active molecules from decoys. Frontiers Media S.A. 2020-12-17 /pmc/articles/PMC7773945/ /pubmed/33392260 http://dx.doi.org/10.3389/fmolb.2020.601065 Text en Copyright © 2020 Holderbach, Adam, Jayaram, Wade and Mukherjee. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Molecular Biosciences
Holderbach, Stefan
Adam, Lukas
Jayaram, B.
Wade, Rebecca C.
Mukherjee, Goutam
RASPD+: Fast Protein-Ligand Binding Free Energy Prediction Using Simplified Physicochemical Features
title RASPD+: Fast Protein-Ligand Binding Free Energy Prediction Using Simplified Physicochemical Features
title_full RASPD+: Fast Protein-Ligand Binding Free Energy Prediction Using Simplified Physicochemical Features
title_fullStr RASPD+: Fast Protein-Ligand Binding Free Energy Prediction Using Simplified Physicochemical Features
title_full_unstemmed RASPD+: Fast Protein-Ligand Binding Free Energy Prediction Using Simplified Physicochemical Features
title_short RASPD+: Fast Protein-Ligand Binding Free Energy Prediction Using Simplified Physicochemical Features
title_sort raspd+: fast protein-ligand binding free energy prediction using simplified physicochemical features
topic Molecular Biosciences
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7773945/
https://www.ncbi.nlm.nih.gov/pubmed/33392260
http://dx.doi.org/10.3389/fmolb.2020.601065
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