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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...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2020
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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. |
format | Online Article Text |
id | pubmed-7773945 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
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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