MuToN Quantifies Binding Affinity Changes upon Protein Mutations by Geometric Deep Learning

Abstract Assessing changes in protein–protein binding affinity due to mutations helps understanding a wide range of crucial biological processes within cells. Despite significant efforts to create accurate computational models, predicting how mutations affect affinity remains challenging due to the...

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Main Authors: Pengpai Li, Zhi‐Ping Liu
Format: Article
Language:English
Published: Wiley 2024-09-01
Series:Advanced Science
Subjects:
Online Access:https://doi.org/10.1002/advs.202402918
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author Pengpai Li
Zhi‐Ping Liu
author_facet Pengpai Li
Zhi‐Ping Liu
author_sort Pengpai Li
collection DOAJ
description Abstract Assessing changes in protein–protein binding affinity due to mutations helps understanding a wide range of crucial biological processes within cells. Despite significant efforts to create accurate computational models, predicting how mutations affect affinity remains challenging due to the complexity of the biological mechanisms involved. In the present work, a geometric deep learning framework called MuToN is introduced for quantifying protein binding affinity change upon residue mutations. The method, designed with geometric attention networks, is mechanism‐aware. It captures changes in the protein binding interfaces of mutated complexes and assesses the allosteric effects of amino acids. Experimental results highlight MuToN's superiority compared to existing methods. Additionally, MuToN's flexibility and effectiveness are illustrated by its precise predictions of binding affinity changes between SARS‐CoV‐2 variants and the ACE2 complex.
format Article
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institution OA Journals
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spelling doaj-art-84e54daee5d249749b642b076d0d9aaf2025-08-20T01:55:16ZengWileyAdvanced Science2198-38442024-09-011135n/an/a10.1002/advs.202402918MuToN Quantifies Binding Affinity Changes upon Protein Mutations by Geometric Deep LearningPengpai Li0Zhi‐Ping Liu1Department of Biomedical Engineering School of Control Science and Engineering Shandong University, Jinan Shandong 250061 ChinaDepartment of Biomedical Engineering School of Control Science and Engineering Shandong University, Jinan Shandong 250061 ChinaAbstract Assessing changes in protein–protein binding affinity due to mutations helps understanding a wide range of crucial biological processes within cells. Despite significant efforts to create accurate computational models, predicting how mutations affect affinity remains challenging due to the complexity of the biological mechanisms involved. In the present work, a geometric deep learning framework called MuToN is introduced for quantifying protein binding affinity change upon residue mutations. The method, designed with geometric attention networks, is mechanism‐aware. It captures changes in the protein binding interfaces of mutated complexes and assesses the allosteric effects of amino acids. Experimental results highlight MuToN's superiority compared to existing methods. Additionally, MuToN's flexibility and effectiveness are illustrated by its precise predictions of binding affinity changes between SARS‐CoV‐2 variants and the ACE2 complex.https://doi.org/10.1002/advs.202402918binding affinitygeometric deep learningmutation
spellingShingle Pengpai Li
Zhi‐Ping Liu
MuToN Quantifies Binding Affinity Changes upon Protein Mutations by Geometric Deep Learning
Advanced Science
binding affinity
geometric deep learning
mutation
title MuToN Quantifies Binding Affinity Changes upon Protein Mutations by Geometric Deep Learning
title_full MuToN Quantifies Binding Affinity Changes upon Protein Mutations by Geometric Deep Learning
title_fullStr MuToN Quantifies Binding Affinity Changes upon Protein Mutations by Geometric Deep Learning
title_full_unstemmed MuToN Quantifies Binding Affinity Changes upon Protein Mutations by Geometric Deep Learning
title_short MuToN Quantifies Binding Affinity Changes upon Protein Mutations by Geometric Deep Learning
title_sort muton quantifies binding affinity changes upon protein mutations by geometric deep learning
topic binding affinity
geometric deep learning
mutation
url https://doi.org/10.1002/advs.202402918
work_keys_str_mv AT pengpaili mutonquantifiesbindingaffinitychangesuponproteinmutationsbygeometricdeeplearning
AT zhipingliu mutonquantifiesbindingaffinitychangesuponproteinmutationsbygeometricdeeplearning