Pentapeptide dimers and multimers

Interestingly, a different trend is observed with Y1 receptors (HEL cells) where an even more substantial enhancement in activity occurs upon dimerization. The activity at this receptor was largely independent of the nature of the tether, with each dimer displaying a 50- 100-fold enhancement relative to the reference monomers. Similar to what was observed in the rat brain assay, the tetra- and hexamer display an additional 20-fold higher activity. 

Results are presented on a per-molecule and not a per-peptide chain basis. Brain and HEL cell asays were carried out as described on Tables 1 and 3, respectively. 

The peptides described in this report suggest a simple model for a minimum, essential pharmacophore that could provide a useful starting point for the design of potent and selective small peptide and non-peptide antagonists. To this end, the structure of the recendy reported NPY antagonist BIBP3226 (Rudolf et aL, 1994) is consistent with this model. 

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