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Supramolecular Approaches for Inhibition of Protein–Protein and Protein–DNA Interactions

Supramolecular Aspects of Chemical Biology

  1. Cooper H. Battle,
  2. Janarthanan Jayawickramarajah

Published Online: 15 MAR 2012

DOI: 10.1002/9780470661345.smc181

Supramolecular Chemistry: From Molecules to Nanomaterials

Supramolecular Chemistry: From Molecules to Nanomaterials

How to Cite

Battle, C. H. and Jayawickramarajah, J. 2012. Supramolecular Approaches for Inhibition of Protein–Protein and Protein–DNA Interactions. Supramolecular Chemistry: From Molecules to Nanomaterials. .

Author Information

  1. Tulane University, New Orleans, LA, USA

Publication History

  1. Published Online: 15 MAR 2012

Abstract

The disruption of protein–protein and protein–DNA interactions is increasingly being realized as important avenues for therapeutic intervention. Unlike the successes observed in the more mature field of small molecule derived active site antagonists, however, the sequestration of the sizeable, solvent exposed, and largely featureless protein surfaces remains a significant challenge. This chapter will provide a detailed account of the types of novel inhibitors being developed that address this challenge, with special emphasis given to supramolecular approaches. Indeed, while still in its infancy, the field of aqueous supramolecular chemistry has made great strides in the development of both covalent and self-assembled multivalent scaffolds for use in protein surface binding. While the former can provide rigid covalent scaffolds tailored for multivalent binding, the latter has the added benefit of being dynamic and thereby can rapidly lead to protein binders that allow for template-driven elucidation, are stimuli-responsive, and able to project heteromeric recognition elements. Taken together, these properties give supramolecular inhibitors the potential for exciting future applications in the disruption of protein interactions.

Keywords:

  • supramolecular;
  • protein–protein interaction;
  • self-assembly;
  • proteomimetics;
  • peptidomimetics;
  • multivalency