22
Development and Validation of a Genetic Algorithm for Flexible Docking Gareth Jones 1 *, Peter Willett 1 , Robert C. Glen 2 , Andrew R. Leach 3 and Robin Taylor 4 1 Department of Information Studies and Krebs Institute for Biomolecular Research, University of Shef®eld, Western Bank, Shef®eld S10 2TN, UK 2 Department of Physical Sciences, Wellcome Foundation Research Laboratories Beckenham, Kent BR3 3BS UK 3 Glaxo Wellcome Medicines Research Centre, Gunnels Wood Road, Stevenage SG1 2NY, UK 4 Cambridge Crystallographic Data Centre, 12 Union Road Cambridge CB2 1EZ, UK Prediction of small molecule binding modes to macromolecules of known three-dimensional structure is a problem of paramount importance in rational drug design (the ``docking'' problem). We report the develop- ment and validation of the program GOLD (Genetic Optimisation for Ligand Docking). GOLD is an automated ligand docking program that uses a genetic algorithm to explore the full range of ligand conformation- al ¯exibility with partial ¯exibility of the protein, and satis®es the funda- mental requirement that the ligand must displace loosely bound water on binding. Numerous enhancements and modi®cations have been applied to the original technique resulting in a substantial increase in the reliability and the applicability of the algorithm. The advanced algorithm has been tested on a dataset of 100 complexes extracted from the Brook- haven Protein DataBank. When used to dock the ligand back into the binding site, GOLD achieved a 71% success rate in identifying the exper- imental binding mode. # 1997 Academic Press Limited Keywords: docking problem; genetic algorithm; molecular recognition; protein ligand docking *Corresponding author Introduction Protein binding sites exhibit highly selective rec- ognition of small organic molecules, in that evol- ution has equipped them with a complex three- dimensional ``lock'' into which only speci®c ``keys'' will ®t. This has been exploited by medicinal che- mists in the design of molecules selectively to aug- ment or retard biochemical pathways and so exhibit a clinical effect. X-ray crystallography has revealed the structure of a signi®cant number of these bind- ing sites. It would be advantageous in attempting the computer-aided design of therapeutic molecules to be able to predict and to explain the binding mode of novel chemical entities (the ``docking'' pro- blem) when the active site geometry is known. Any solution to the docking problem requires both a powerful search technique to explore the conformation space available to the protein and the ligand and a good understanding of the process of molecular recognition to devise scoring functions that can reliably predict binding modes. Further- more, since many putative dockings will require evaluation before elucidating the binding mode, any scoring function must be rapid in operation. There are currently many different approaches to solving the docking problem (Blaney & Dixon, 1993; Jones & Willett, 1995). Early approaches to ligand docking consider both protein and ligand to be rigid, as typi®ed by the DOCK program (Kuntz et al., 1982). Since the bioactive conformation of a bound ligand rarely corresponds to the isolated ligand X-ray structure (Nicklaus et al., 1995), recent techniques have dealt with the issue of confor- mational ¯exibility. Deterministic approaches in- clude the FLOG system of Miller et al. (1994) and FLEXX of Rarey et al. (1996). The latter algorithm is very ef®cient and has been veri®ed on 19 protein- ligand complexes. Alternative, stochastic sampling techniques include genetic algorithms (Jones et al., 1995a; Judson et al., 1994; Oshiro et al., 1995), simu- lated annealing (Goodsell & Olsen, 1990) and evol- utionary programming (Gehlhaar et al., 1995). Inspection of the X-ray crystallographic struc- tures of proteins with associated high-af®nity Present address: R. C. Glen, Tripos Inc., 1699 South Hanley Road, St Louis, MO 63144, USA Abbreviations used: GA, genetic algorithm; PDB, Protein Data Bank; DHFR, dihydrofolate reductase; CSD, Cambridge Structural Database; IMPT, inter- molecular perturbation theory. J. Mol. Biol. (1997) 267, 727±748 0022 ± 2836/97/130727±22 $25.00/0/mb960897 # 1997 Academic Press Limited

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