par Langer, Ingrid 
;Grégoire, Françoise ;Nachtergael, Ingrid ;De Neef, Philippe ;Vertongen, Pascale ;Robberecht, Patrick
Référence Peptides, 25, 2, page (275-278)
Publication Publié, 2004-02
;Grégoire, Françoise ;Nachtergael, Ingrid ;De Neef, Philippe ;Vertongen, Pascale ;Robberecht, Patrick Référence Peptides, 25, 2, page (275-278)
Publication Publié, 2004-02
Article révisé par les pairs
| Résumé : | We synthesized a VIP analog that combines mutations that decrease the affinity for the VPAC1 receptor but maintain a high affinity for the VPAC2 receptor with an amino-terminal hexanoylation that increases the affinity for the VPAC2 receptor with a limited decrease in the affinity of the VPAC1 receptor. The resulting Hexanoyl[A19,K(27,28)]VIP had the expected properties of a high affinity for the VPAC2 receptor and a low affinity for the VPAC1 receptor and also a low affinity for the PAC1 and secretin receptors. With a 1000-fold preference for the VPAC2 receptor and a IC50 value of binding of 1 nM, this compound is the most potent and the most selective agonist presently described. |
