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We present the protolysis-targeting chimera (PROTAC) Conformer Generator, a fast and knowledge-based tool for generating robust conformational ensembles of PROTACs and other chimeric degraders. The modeling protocol integrates conformer generation, rigid-body ternary complex (TC) assembly, and conformational sampling strategies that address the inherent flexibility and complexity of these molecules. Each modeled TC is evaluated using a clash-score and a surface-score, designed to prioritize sterically and geometrically plausible models with favorable protein surface interactions. The protocol was validated using experimentally determined PROTAC-mediated TC structures from the Protein Data Bank and "PROTAC-like" structures from the Cambridge Structural Database, demonstrating accuracy across diverse systems. The results show that the PROTAC Conformer Generator can reliably reproduce experimental conformations and generate simple TC models that recapitulate the relative orientations between E3 ubiquitin ligase and the protein of interest as observed in protein crystal structures. This robust validation supports the method's reliability and establishes a reference framework for degrader modeling studies. The PROTAC Conformer Generator provides a structured and validated workflow for modeling and assessing degrader conformations and ternary complexes, enabling rapid ensemble generation and downstream integration into relevant early stage drug design pipelines.
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http://dx.doi.org/10.1021/acs.jcim.5c00880 | DOI Listing |
J Chem Inf Model
September 2025
Cambridge Crystallographic Data Centre, 12 Union Road, Cambridge CB2 1EZ, U.K.
We present the protolysis-targeting chimera (PROTAC) Conformer Generator, a fast and knowledge-based tool for generating robust conformational ensembles of PROTACs and other chimeric degraders. The modeling protocol integrates conformer generation, rigid-body ternary complex (TC) assembly, and conformational sampling strategies that address the inherent flexibility and complexity of these molecules. Each modeled TC is evaluated using a clash-score and a surface-score, designed to prioritize sterically and geometrically plausible models with favorable protein surface interactions.
View Article and Find Full Text PDFJ Med Chem
August 2025
Boehringer Ingelheim RCV GmbH Co KG, Dr. Boehringer-Gasse 5-11, Vienna 1121, Austria.
In this study, we profiled 11 structurally related von Hippel-Lindau (VHL)-based proteolysis-targeting chimeras (PROTACs), evaluating pharmacokinetics in mice (oral bioavailability and clearance), ADME properties (solubility, permeability, and efflux ratio), and key physicochemical traits (polarity, lipophilicity, and chameleonicity). While Caco-2 permeability did not correlate with oral bioavailability (F%), the efflux ratio (ER) proved a strong predictor. The ER could also be estimated using the chromatographic descriptor log k'80 PLRP-S.
View Article and Find Full Text PDFCommun Biol
July 2025
Structural Genomics Consortium, University of Toronto, Toronto, ON, Canada.
Human DCAF1 is a multidomain protein that plays a critical role in protein homeostasis. Its WDR domain functions as a substrate recruitment module for RING-type CRL4 and HECT family EDVP E3 ubiquitin ligases, enabling the ubiquitination and proteasomal degradation of specific substrates. DCAF1's activity has been implicated in cell proliferation and is documented to promote tumorigenesis.
View Article and Find Full Text PDFJ Comput Aided Mol Des
July 2025
Integrated Drug Discovery, Aragen Lifesciences Ltd, Hyderabad, 500076, India.
Targeted protein degradation by proteolysis-targeting chimeras (PROTAC) is dependent on formation and plasticity of ternary complexes enabling ubiquitination. In this study, we employed long-timescale molecular dynamics (MD) simulations, free energy landscape analysis, and quantum mechanical (QM) calculations to investigate the molecular determinants of PROTAC efficacy. Using three model systems (FAK-VHL, BTK-CRBN, and TTK-CRBN), each with three PROTACs of varying potencies, we analyzed a total of nine ternary complexes over 500 ns MD simulations each.
View Article and Find Full Text PDFTargeted protein degradation via PROTACs offers a promising therapeutic strategy, yet accurate modeling of ternary complexes remains a critical challenge in degrader design. In this study, we systematically benchmark two leading structure prediction tools, AlphaFold3 and PRosettaC, against a curated dataset of 36 crystallographically resolved ternary complexes. Using DockQ as a quantitative interface scoring metric, we assess the structural fidelity of predicted complexes under both scaffold-inclusive and stripped configurations.
View Article and Find Full Text PDF