Journal of Computer-Aided Molecular Design

, Volume 8, Issue 5, pp 513–525

Electrostatic complementarity between proteins and ligands. 1. Charge disposition, dielectric and interface effects

  • P. -L. Chau
  • P. M. Dean
Research Papers

DOI: 10.1007/BF00123663

Cite this article as:
Chau, P.L. & Dean, P.M. J Computer-Aided Mol Des (1994) 8: 513. doi:10.1007/BF00123663


Electrostatic interactions have always been considered an important factor governing ligand-receptor interactions. Previous work in this field has established the existence of electrostatic complementarity between the ligand and its receptor site. However, this property has not been treated rigorously, and the description remains largely qualitative. In this work, 34 data sets of high quality were chosen from the Brookhaven Protein Databank. The electrostatic complementarity has been calculated between the surface potentials; complementarity is absent between adjacent or neighbouring atoms of the ligand and the receptor. There is little difference between complementarities on the total ligand surface and the interfacial region. Altering the homogeneous dielectric to distance-dependent dielectrics reduces the complementarity slightly, but does not affect the pattern of complementarity.

Key words

Drug design Molecular electrostatic potential MEP Dielectric 

Copyright information

© ESCOM Science Publishers B.V 1994

Authors and Affiliations

  • P. -L. Chau
    • 1
  • P. M. Dean
    • 1
  1. 1.Department of PharmacologyUniversity of CambridgeCambridgeU.K.