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Issue 23, 2006
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Reinforced molecular recognition as an alternative to rigid receptors

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Abstract

In theory, a perfectly rigid receptor will probably be an unbeatable binder. However, rigidity may not be easy to achieve in practice and it is certainly not Nature's method to realise high affinity. In many proteins binding affinity is increased through non-covalent interactions within the protein. Thus there is a considerable incentive to follow Nature's example and start exploring the use of secondary intra-receptor interactions to aid in the binding process. Secondary interactions within a receptor will reinforce host–guest binding when the same conformational rearrangement (or freezing of motion) is required for guest binding as for the formation of the intra-receptor interactions. Introducing secondary interactions will require rather elaborate synthetic receptors to be produced. With the recent developments in dynamic combinatorial chemistry, access to the desired structures should be facilitated. Whether or not this approach will develop into a practical method remains to be established, but even if it does not, efforts along these lines will lead to a better understanding of the complex interplay between molecular recognition, folding and dynamics.

Graphical abstract: Reinforced molecular recognition as an alternative to rigid receptors

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Publication details

The article was received on 07 Nov 2005, accepted on 18 Jan 2006 and first published on 08 May 2006


Article type: Paper
DOI: 10.1039/B515817F
Citation: Dalton Trans., 2006,0, 2861-2864
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    Reinforced molecular recognition as an alternative to rigid receptors

    S. Otto, Dalton Trans., 2006, 0, 2861
    DOI: 10.1039/B515817F

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