FlexSBDD: Structure-Based Drug Design with Flexible Protein Modeling
Structure-based drug design (SBDD), which aims to generate 3D ligand molecules binding to target proteins, is a fundamental task in drug discovery. Existing SBDD methods typically treat protein as rigid and neglect protein structural change when binding with ligand molecules, leading to a big gap wi...
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creator | Zhang, Zaixi Wang, Mengdi Liu, Qi |
description | Structure-based drug design (SBDD), which aims to generate 3D ligand
molecules binding to target proteins, is a fundamental task in drug discovery.
Existing SBDD methods typically treat protein as rigid and neglect protein
structural change when binding with ligand molecules, leading to a big gap with
real-world scenarios and inferior generation qualities (e.g., many steric
clashes). To bridge the gap, we propose FlexSBDD, a deep generative model
capable of accurately modeling the flexible protein-ligand complex structure
for ligand molecule generation. FlexSBDD adopts an efficient flow matching
framework and leverages E(3)-equivariant network with scalar-vector dual
representation to model dynamic structural changes. Moreover, novel data
augmentation schemes based on structure relaxation/sidechain repacking are
adopted to boost performance. Extensive experiments demonstrate that FlexSBDD
achieves state-of-the-art performance in generating high-affinity molecules and
effectively modeling the protein's conformation change to increase favorable
protein-ligand interactions (e.g., Hydrogen bonds) and decrease steric clashes. |
doi_str_mv | 10.48550/arxiv.2409.19645 |
format | Article |
fullrecord | <record><control><sourceid>arxiv_GOX</sourceid><recordid>TN_cdi_arxiv_primary_2409_19645</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2409_19645</sourcerecordid><originalsourceid>FETCH-arxiv_primary_2409_196453</originalsourceid><addsrcrecordid>eNpjYJA0NNAzsTA1NdBPLKrILNMzMjGw1DO0NDMx5WRwcctJrQh2cnGxUgguKSpNLiktStV1SixOTVFwKSpNV3BJLc5Mz1MozyzJUAApzUzKSVUIKMovSc3MU_DNT0nNycxL52FgTUvMKU7lhdLcDPJuriHOHrpg--ILijJzE4sq40H2xoPtNSasAgCCGjd2</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>FlexSBDD: Structure-Based Drug Design with Flexible Protein Modeling</title><source>arXiv.org</source><creator>Zhang, Zaixi ; Wang, Mengdi ; Liu, Qi</creator><creatorcontrib>Zhang, Zaixi ; Wang, Mengdi ; Liu, Qi</creatorcontrib><description>Structure-based drug design (SBDD), which aims to generate 3D ligand
molecules binding to target proteins, is a fundamental task in drug discovery.
Existing SBDD methods typically treat protein as rigid and neglect protein
structural change when binding with ligand molecules, leading to a big gap with
real-world scenarios and inferior generation qualities (e.g., many steric
clashes). To bridge the gap, we propose FlexSBDD, a deep generative model
capable of accurately modeling the flexible protein-ligand complex structure
for ligand molecule generation. FlexSBDD adopts an efficient flow matching
framework and leverages E(3)-equivariant network with scalar-vector dual
representation to model dynamic structural changes. Moreover, novel data
augmentation schemes based on structure relaxation/sidechain repacking are
adopted to boost performance. Extensive experiments demonstrate that FlexSBDD
achieves state-of-the-art performance in generating high-affinity molecules and
effectively modeling the protein's conformation change to increase favorable
protein-ligand interactions (e.g., Hydrogen bonds) and decrease steric clashes.</description><identifier>DOI: 10.48550/arxiv.2409.19645</identifier><language>eng</language><subject>Quantitative Biology - Biomolecules</subject><creationdate>2024-09</creationdate><rights>http://creativecommons.org/licenses/by/4.0</rights><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>228,230,777,882</link.rule.ids><linktorsrc>$$Uhttps://arxiv.org/abs/2409.19645$$EView_record_in_Cornell_University$$FView_record_in_$$GCornell_University$$Hfree_for_read</linktorsrc><backlink>$$Uhttps://doi.org/10.48550/arXiv.2409.19645$$DView paper in arXiv$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhang, Zaixi</creatorcontrib><creatorcontrib>Wang, Mengdi</creatorcontrib><creatorcontrib>Liu, Qi</creatorcontrib><title>FlexSBDD: Structure-Based Drug Design with Flexible Protein Modeling</title><description>Structure-based drug design (SBDD), which aims to generate 3D ligand
molecules binding to target proteins, is a fundamental task in drug discovery.
Existing SBDD methods typically treat protein as rigid and neglect protein
structural change when binding with ligand molecules, leading to a big gap with
real-world scenarios and inferior generation qualities (e.g., many steric
clashes). To bridge the gap, we propose FlexSBDD, a deep generative model
capable of accurately modeling the flexible protein-ligand complex structure
for ligand molecule generation. FlexSBDD adopts an efficient flow matching
framework and leverages E(3)-equivariant network with scalar-vector dual
representation to model dynamic structural changes. Moreover, novel data
augmentation schemes based on structure relaxation/sidechain repacking are
adopted to boost performance. Extensive experiments demonstrate that FlexSBDD
achieves state-of-the-art performance in generating high-affinity molecules and
effectively modeling the protein's conformation change to increase favorable
protein-ligand interactions (e.g., Hydrogen bonds) and decrease steric clashes.</description><subject>Quantitative Biology - Biomolecules</subject><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><sourceid>GOX</sourceid><recordid>eNpjYJA0NNAzsTA1NdBPLKrILNMzMjGw1DO0NDMx5WRwcctJrQh2cnGxUgguKSpNLiktStV1SixOTVFwKSpNV3BJLc5Mz1MozyzJUAApzUzKSVUIKMovSc3MU_DNT0nNycxL52FgTUvMKU7lhdLcDPJuriHOHrpg--ILijJzE4sq40H2xoPtNSasAgCCGjd2</recordid><startdate>20240929</startdate><enddate>20240929</enddate><creator>Zhang, Zaixi</creator><creator>Wang, Mengdi</creator><creator>Liu, Qi</creator><scope>ALC</scope><scope>GOX</scope></search><sort><creationdate>20240929</creationdate><title>FlexSBDD: Structure-Based Drug Design with Flexible Protein Modeling</title><author>Zhang, Zaixi ; Wang, Mengdi ; Liu, Qi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-arxiv_primary_2409_196453</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>Quantitative Biology - Biomolecules</topic><toplevel>online_resources</toplevel><creatorcontrib>Zhang, Zaixi</creatorcontrib><creatorcontrib>Wang, Mengdi</creatorcontrib><creatorcontrib>Liu, Qi</creatorcontrib><collection>arXiv Quantitative Biology</collection><collection>arXiv.org</collection></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>Zhang, Zaixi</au><au>Wang, Mengdi</au><au>Liu, Qi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>FlexSBDD: Structure-Based Drug Design with Flexible Protein Modeling</atitle><date>2024-09-29</date><risdate>2024</risdate><abstract>Structure-based drug design (SBDD), which aims to generate 3D ligand
molecules binding to target proteins, is a fundamental task in drug discovery.
Existing SBDD methods typically treat protein as rigid and neglect protein
structural change when binding with ligand molecules, leading to a big gap with
real-world scenarios and inferior generation qualities (e.g., many steric
clashes). To bridge the gap, we propose FlexSBDD, a deep generative model
capable of accurately modeling the flexible protein-ligand complex structure
for ligand molecule generation. FlexSBDD adopts an efficient flow matching
framework and leverages E(3)-equivariant network with scalar-vector dual
representation to model dynamic structural changes. Moreover, novel data
augmentation schemes based on structure relaxation/sidechain repacking are
adopted to boost performance. Extensive experiments demonstrate that FlexSBDD
achieves state-of-the-art performance in generating high-affinity molecules and
effectively modeling the protein's conformation change to increase favorable
protein-ligand interactions (e.g., Hydrogen bonds) and decrease steric clashes.</abstract><doi>10.48550/arxiv.2409.19645</doi><oa>free_for_read</oa></addata></record> |
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subjects | Quantitative Biology - Biomolecules |
title | FlexSBDD: Structure-Based Drug Design with Flexible Protein Modeling |
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