This study proposes the synthesis and spectroscopic studies of new host molecules designed to possess a spherically-shaped cleft-like cavity with multipoint interactions in a three-dimensional array for the recognition and binding of peptide and carbohydrate substrates. These compounds will provide models for substrate recognition and binding of proteins as well as cell surface recognition processes. In particular, we are interested in binding an important portion of the active site of the HlV-l aspartic protease, the aspartyl-threonyl-glycine trimer. The multiple contact points will include some of those found in the natural protein receptors which are amino acid side chain carboxylates (aspartate, glutamate), alcohols (serine, tyrosine) and amides (asparagine, glutamine). These binding groups will provide a more biological-like environment for the binding of the peptides and carbohydrates, while their incorporation into a well-defined synthetic host allows for monitoring of specific molecular interactions. Some hosts will also have from twelve to sixteen hydroxyl groups as additional contact points for binding.
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