Journal of Chemical Theory and Computation · 2020 · 44 citations · 62 references
PharmacyChemistryMedicinal ChemistryComputational ChemistryComputational Medicinal ChemistryDrug DiscoveryBinding Affinity PredictionComputational Drug DiscoveryLigand BindingMolecular ModelingProtein-ligand DockingAccuracy-computational Cost TradeoffEnhanced SamplingEpoxide HydrolasesHamiltonian Replica ExchangeLigand-target Interaction ModelingMetadynamicsProtein-ligand Binding Free Energy CalculationsProtein-ligand Complex Modeling
Calculating absolute binding free energies is challenging and important. In this paper, we test some recently developed metadynamics-based methods and develop a new combination with a Hamiltonian replica-exchange approach. The methods were tested on 18 chemically diverse ligands with a wide range of different binding affinities to a complex target; namely, human soluble epoxide hydrolase. The results suggest that metadynamics with a funnel-shaped restraint can be used to calculate, in a computationally affordable and relatively accurate way, the absolute binding free energy for small fragments. When used in combination with an optimal pathlike variable obtained using machine learning or with the Hamiltonian replica-exchange algorithm SWISH, this method can achieve reasonably accurate results for increasingly complex ligands, with a good balance of computational cost and speed. An additional benefit of using the combination of metadynamics and SWISH is that it also provides useful information about the role of water in the binding mechanism.
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Canonical sampling through velocity rescaling
Giovanni Bussi, Davide Donadio, Michele Parrinello · The Journal of Chemical Physics · 2007 · 18.4K citations · Full text
Natural Sciences, Chemistry, Physics +17
CHARMM36m: an improved force field for folded and intrinsically disordered proteins
Jing Huang, Sarah Rauscher, Grzegorz Nawrocki et al. · Nature Methods · 2016 · 7.6K citations · Full text