Protein-Ligand Interactions as the Basis for Drug Action

Conference paper
Part of the NATO Science for Peace and Security Series A: Chemistry and Biology book series (NAPSA)

Abstract

Lead optimization seeks for conclusive parameters beyond affinity to profile drug-receptor binding. One option is to use thermodynamic signatures since different targets require different mode-of-action mechanisms. Since thermodynamic properties are influenced by multiple factors such as interactions, desolvation, residual mobility, dynamics, or local water structure, careful analysis is essential to define the reference point why a particular signature is given and how it can subsequently be optimized. Relative comparisons of congeneric ligand pairs along with access to structural information allow factorizing a thermodynamic signature into individual contributions.

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Copyright information

© Springer Science+Business Media Dordrecht 2015

Authors and Affiliations

  1. 1.Department of Pharmaceutical ChemistryUniversity of MarburgMarburgGermany

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