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Issue 36, 2016
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Towards vast libraries of scaffold-diverse, conformationally constrained oligomers

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Abstract

There is great interest in the development of probe molecules and drug leads that would bind tightly and selectively to protein surfaces that are difficult to target with traditional molecules, such as those involved in protein–protein interactions. The currently available evidence suggests that this will require molecules that are larger and have quite different chemical properties than typical Lipinski-compliant molecules that target enzyme active sites. We describe here efforts to develop vast libraries of conformationally constrained oligomers as a potentially rich source of these molecules.

Graphical abstract: Towards vast libraries of scaffold-diverse, conformationally constrained oligomers

  • This article is part of the themed collection: Foldamers
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Publication details

The article was received on 21 Jan 2016, accepted on 08 Mar 2016 and first published on 21 Mar 2016


Article type: Feature Article
DOI: 10.1039/C6CC00617E
Citation: Chem. Commun., 2016,52, 6038-6059
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    Towards vast libraries of scaffold-diverse, conformationally constrained oligomers

    T. Kodadek and P. J. McEnaney, Chem. Commun., 2016, 52, 6038
    DOI: 10.1039/C6CC00617E

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