Electrostatic complementarity between proteins and ligands. 3. Structural basis.

P L Chau; P M Dean

doi:10.1007/bf00123665

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Electrostatic complementarity between proteins and ligands. 3. Structural basis.

P L Chau·P M Dean

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Abstract

Electrostatic potential complementarity between ligands and their receptor sites is evaluated by the superposition of the electrostatic potential, generated by the receptor, onto the ligand potential over the ligand van der Waals surface. We would like to examine which structural factors generate this pattern of superposition. Example studies suggest that in many ligand-protein pairs, there exist principal formal charges on each molecule, largely responsible for the electrostatic potential complementarity observed. Electrostatic potential complementarity depends on the relative disposition of these principal charges and the ligand van der Waals surface. Simple mathematical models were constructed to predict the complementarity solely from structural considerations. The essential conditions for electrostatic potential complementarity were elucidated. These can be used in ligand design strategies to obtain an electrostatically optimal ligand.

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Amino Acid Sequence Binding Sites Computer-Aided Design Drug Design Electrochemistry Humans Ligands Models, Chemical Models, Molecular Molecular Sequence Data Molecular Structure Oligopeptides Proteins Journal Article Research Support, Non-U.S. Gov't

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P L Chau, P M Dean. 1994. Electrostatic complementarity between proteins and ligands. 3. Structural basis.. https://doi.org/10.1007/bf00123665

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