Abstract
The extraordinary high binding affinities and selectivities of natural receptors arises from the cooperative action of small rigid peptide sub-units oriented in a 3D fashion around the target molecule. Efforts to mimic such functional group arrays in synthetic systems have led to the synthesis of artificial protein receptors mimicking the binding properties of natural antibodies. Similar studies on the self-assembly of polar functionalities using noncovalent platforms has so far received very little attention. In this paper, we describe a novel approach towards the synthesis of synthetic antibody mimics, making use of noncovalent platforms for the self-assembly of small rigid peptide fragments.
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