The maximal affinity of ligands.

We explore the question of what are the best ligands for macromolecular targets. A survey of experimental data on a large number of the strongest-binding ligands indicates that the free energy of binding increases with the number of nonhydrogen atoms with an initial slope of approximately -1.5 kcal/mol (1 cal = 4.18 J) per atom. For ligands that contain more than 15 nonhydrogen atoms, the free energy of binding increases very little with relative molecular mass. This nonlinearity is largely ascribed to nonthermodynamic factors. An analysis of the dominant interactions suggests that van der Waals interactions and hydrophobic effects provide a reasonable basis for understanding binding affinities across the entire set of ligands. Interesting outliers that bind unusually strongly on a per atom basis include metal ions, covalently attached ligands, and a few well known complexes such as biotin-avidin.

[1]  S. Maestas,et al.  The thermodynamics of absorption of xenon by myoglobin. , 1970, The Journal of physical chemistry.

[2]  L. Parkhurst Hemoglobin and Myoglobin Ligand Kinetics , 1979 .

[3]  Charles Tanford,et al.  The hydrophobic effect , 1980 .

[4]  P. Andrews,et al.  Functional group contributions to drug-receptor interactions. , 1984, Journal of medicinal chemistry.

[5]  J. Schloss Comparative affinities of the epimeric reaction-intermediate analogs 2- and 4-carboxy-D-arabinitol 1,5-bisphosphate for spinach ribulose 1,5-bisphosphate carboxylase. , 1988, The Journal of biological chemistry.

[6]  H. Zollner,et al.  Handbook of Enzyme Inhibitors , 1989 .

[7]  K A Dill,et al.  The meaning of hydrophobicity. , 1990, Science.

[8]  P. Bartlett,et al.  Synthesis and evaluation of an inhibitor of carboxypeptidase A with a Ki value in the femtomolar range. , 1991, Biochemistry.

[9]  J. Knowles,et al.  Enzyme catalysis: not different, just better , 1991, Nature.

[10]  B Honig,et al.  Reconciling the magnitude of the microscopic and macroscopic hydrophobic effects. , 1991, Science.

[11]  P A Kollman,et al.  Absolute and relative binding free energy calculations of the interaction of biotin and its analogs with streptavidin using molecular dynamics/free energy perturbation approaches , 1993, Proteins.

[12]  P A Kollman,et al.  What determines the strength of noncovalent association of ligands to proteins in aqueous solution? , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[13]  G. Rogers,et al.  Kinetic and equilibrium characterization of vesamicol receptor-ligand complexes with picomolar dissociation constants. , 1993, Molecular pharmacology.

[14]  J. D. Karkas,et al.  Zaragozic acids: a family of fungal metabolites that are picomolar competitive inhibitors of squalene synthase. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[15]  A. Duranti,et al.  2-Substituted 5-methoxy-N-acyltryptamines: synthesis, binding affinity for the melatonin receptor, and evaluation of the biological activity. , 1993, Journal of medicinal chemistry.

[16]  D. Quinn,et al.  m-(N,N,N-Trimethylammonio)trifluoroacetophenone: a femtomolar inhibitor of acetylcholinesterase , 1993 .

[17]  M Karplus,et al.  HOOK: A program for finding novel molecular architectures that satisfy the chemical and steric requirements of a macromolecule binding site , 1994, Proteins.

[18]  P. Kollman,et al.  A Second Generation Force Field for the Simulation of Proteins, Nucleic Acids, and Organic Molecules , 1995 .

[19]  T. Halgren,et al.  A priori prediction of activity for HIV-1 protease inhibitors employing energy minimization in the active site. , 1995, Journal of medicinal chemistry.

[20]  N. Allegretto,et al.  Development of potent thrombin receptor antagonist peptides. , 1996, Journal of medicinal chemistry.

[21]  E. Shakhnovich,et al.  SMoG: de Novo Design Method Based on Simple, Fast, and Accurate Free Energy Estimates. 1. Methodology and Supporting Evidence , 1996 .

[22]  William L. Jorgensen,et al.  PERFORMANCE OF THE AMBER94, MMFF94, AND OPLS-AA FORCE FIELDS FOR MODELING ORGANIC LIQUIDS , 1996 .

[23]  J. C. Dyason,et al.  A study of the active site of influenza virus sialidase: an approach to the rational design of novel anti-influenza drugs. , 1996, Journal of medicinal chemistry.

[24]  K D Stewart,et al.  A novel, picomolar inhibitor of human immunodeficiency virus type 1 protease. , 1996, Journal of medicinal chemistry.

[25]  P. Hajduk,et al.  Discovering High-Affinity Ligands for Proteins: SAR by NMR , 1996, Science.

[26]  G. Rigdon,et al.  Synthesis and evaluation of heterocyclic carboxamides as potential antipsychotic agents. , 1996, Journal of medicinal chemistry.

[27]  5-HT1D receptor agonist properties of novel 2-[5-[[(trifluoromethyl)sulfonyl]oxy]indolyl]ethylamines and their use as synthetic intermediates. , 1996, Journal of medicinal chemistry.

[28]  S. Adelstein,et al.  [125I/127I]iodoHoechst 33342: synthesis, DNA binding, and biodistribution. , 1996, Journal of medicinal chemistry.

[29]  W. Howe,et al.  Structure-based design of HIV protease inhibitors: sulfonamide-containing 5,6-dihydro-4-hydroxy-2-pyrones as non-peptidic inhibitors. , 1996, Journal of medicinal chemistry.

[30]  New series of potent, orally bioavailable, non-peptidic cyclic sulfones as HIV-1 protease inhibitors. , 1996, Journal of medicinal chemistry.

[31]  W J Dunn,et al.  Solution of the conformation and alignment tensors for the binding of trimethoprim and its analogs to dihydrofolate reductase: 3D-quantitative structure-activity relationship study using molecular shape analysis, 3-way partial least-squares regression, and 3-way factor analysis. , 1996, Journal of medicinal chemistry.

[32]  HIV protease inhibitory bis-benzamide cyclic ureas: a quantitative structure-activity relationship analysis. , 1996, Journal of medicinal chemistry.

[33]  Chong-Hwan Chang,et al.  Cyclic HIV protease inhibitors: synthesis, conformational analysis, P2/P2' structure-activity relationship, and molecular recognition of cyclic ureas. , 1996, Journal of medicinal chemistry.

[34]  Design, synthesis, and evaluation of nonpeptidic inhibitors of human rhinovirus 3C protease. , 1996, Journal of medicinal chemistry.

[35]  Anti-inflammatory 17β-Thioalkyl-16α,17α-ketal and -acetal Androstanes: A New Class of Airway Selective Steroids for the Treatment of Asthma , 1996 .

[36]  C. E. Peishoff,et al.  Potent, selective, orally active 3-oxo-1,4-benzodiazepine GPIIb/IIIa integrin antagonists. , 1996, Journal of medicinal chemistry.

[37]  Thomas Lengauer,et al.  A fast flexible docking method using an incremental construction algorithm. , 1996, Journal of molecular biology.

[38]  P. Pauwels,et al.  Serotonin dimers: application of the bivalent ligand approach to the design of new potent and selective 5-HT(1B/1D) agonists. , 1996, Journal of medicinal chemistry.

[39]  M. Kuhar,et al.  Halogenated mazindol analogs as potential inhibitors of the cocaine binding site at the dopamine transporter. , 1996, Journal of medicinal chemistry.

[40]  I D Kuntz,et al.  Structure-based design and combinatorial chemistry yield low nanomolar inhibitors of cathepsin D. , 1997, Chemistry & biology.

[41]  F. Lombardo,et al.  Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings , 1997 .

[42]  K A Dill,et al.  Additivity Principles in Biochemistry* , 1997, The Journal of Biological Chemistry.

[43]  Ajay,et al.  Can we learn to distinguish between "drug-like" and "nondrug-like" molecules? , 1998, Journal of medicinal chemistry.

[44]  Robert M. Stroud,et al.  Design of potent selective zinc-mediated serine protease inhibitors , 1998, Nature.

[45]  Peter J. Rossky,et al.  Surface topography dependence of biomolecular hydrophobic hydration , 1998, Nature.

[46]  B Tidor,et al.  Computation of electrostatic complements to proteins: A case of charge stabilized binding , 1998, Protein science : a publication of the Protein Society.