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Gourlet, P. et al.

Vasoactive intestinal peptide modification at position 22 allows discrimination between receptor subtypes.

Secretin and growth hormone releasing factor (GRF) have a weak affinity for VIP (vasoactive intestinal peptide)/PACAP (pituitary adenylate cyclase activating polypeptide) receptors, but discriminate between VIP1/PACAP and VIP2/PACAP receptors. This previously allowed us to develop modified secretin and GRF derivatives as high affinity and highly selective VIP1/PACAP receptor ligands. We tested the hypothesis that the presence of a Gln residue at position 24 and a Leu residue at position 22 was responsible for their VIP1/PACAP receptor selectivity. [Gln24]VIP was not different from VIP but [Leu22]VIP had a 100-fold lower affinity for VIP2/PACAP receptors as compared to VIP1/PACAP receptors. The substitution of Tyr22 by Phe22 in VIP had no significant effect on the recognition of both receptors but [Ala22]VIP had a reduced affinity for the VIP2/PACAP receptor. This indicated that an aromatic residue at position 22 of VIP was required for a high affinity for the VIP2/PACAP receptor but not for the VIP1/PACAP receptor.[1]

References

Vasoactive intestinal peptide modification at position 22 allows discrimination between receptor subtypes. Gourlet, P., Vandermeers-Piret, M.C., Rathé, J., De Neef, P., Cnudde, J., Robberecht, P., Waelbroeck, M. Eur. J. Pharmacol. (1998) [Pubmed]

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