DEL-Dock: Molecular Docking-Enabled Modeling of DNA-Encoded Libraries

码头 计算机科学 概率逻辑 计算生物学 对接(动物) 蛋白质数据库 人工智能 结合亲和力 数据挖掘 机器学习 蛋白质结构 化学 生物 遗传学 生物化学 医学 护理部 受体
作者
Kirill Shmilovich,Benson Chen,Theofanis Karaletsos,Mohammad M. Sultan
出处
期刊:Journal of Chemical Information and Modeling [American Chemical Society]
卷期号:63 (9): 2719-2727 被引量:4
标识
DOI:10.1021/acs.jcim.2c01608
摘要

DNA-encoded library (DEL) technology has enabled significant advances in hit identification by enabling efficient testing of combinatorially generated molecular libraries. DEL screens measure protein binding affinity though sequencing reads of molecules tagged with unique DNA barcodes that survive a series of selection experiments. Computational models have been deployed to learn the latent binding affinities that are correlated to the sequenced count data; however, this correlation is often obfuscated by various sources of noise introduced in its complicated data-generation process. In order to denoise DEL count data and screen for molecules with good binding affinity, computational models require the correct assumptions in their modeling structure to capture the correct signals underlying the data. Recent advances in DEL models have focused on probabilistic formulations of count data, but existing approaches have thus far been limited to only utilizing 2-D molecule-level representations. We introduce a new paradigm, DEL-Dock, that combines ligand-based descriptors with 3-D spatial information from docked protein-ligand complexes. 3-D spatial information allows our model to learn over the actual binding modality rather than using only structure-based information of the ligand. We show that our model is capable of effectively denoising DEL count data to predict molecule enrichment scores that are better correlated with experimental binding affinity measurements compared to prior works. Moreover, by learning over a collection of docked poses we demonstrate that our model, trained only on DEL data, implicitly learns to perform good docking pose selection without requiring external supervision from expensive-to-source protein crystal structures.

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