Abstract
We synthesized a VIP analog that combines mutations that decrease the affinity for the VPAC 1 receptor but maintain a high affinity for the VPAC 2 receptor with an amino-terminal hexanoylation that increases the affinity for the VPAC 2 receptor with a limited decrease in the affinity of the VPAC 1 receptor. The resulting Hexanoyl[A 19,K 27,28]VIP had the expected properties of a high affinity for the VPAC 2 receptor and a low affinity for the VPAC 1 receptor and also a low affinity for the PAC 1 and secretin receptors. With a 1000-fold preference for the VPAC 2 receptor and a IC 50 value of binding of 1 nM, this compound is the most potent and the most selective agonist presently described.
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