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In this study, we tested the biological activity of a novel acylated form of (Pro 3 )glucose-dependent insulinotropic polypetide [(Pro 3 )GIP] prepared by conjugating palmitic acid to Lys 16  to enhance its efficacy  in vivo  by promoting binding to albumin and extending its biological actions. Like the parent molecule (Pro 3 )GIP, (Pro 3 )GIPLys 16 PAL was completely stable to the actions of DPP-IV and significantly ( p &lt;0.01 to  p &lt;0.001) inhibited GIP-stimulated cAMP production and cellular insulin secretion. Furthermore, acute administration of (Pro 3 )GIPLys 16 PAL also significantly ( p &lt;0.05 to  p &lt;0.001) countered the glucose-lowering and insulin-releasing actions of GIP in  ob/ob  mice. Daily injection of (Pro 3 )GIPLys 16 PAL (25 nmol/kg bw) in 14–18-week-old  ob/ob  mice over 14 days had no effect on body weight, food intake or non-fasting plasma glucose and insulin concentrations. (Pro 3 )GIPLys 16 PAL treatment also failed to significantly alter the glycaemic response to an i.p. glucose load or test meal, but insulin concentrations were significantly reduced (1.5-fold;  p &lt;0.05) after the glucose load. Insulin sensitivity was enhanced (1.3-fold;  p &lt;0.05) and pancreatic insulin was significantly reduced ( p &lt;0.05) in the (Pro 3 )GIPLys 16 PAL-treated mice. These data demonstrate that acylation of Lys 16  with palmitic acid in (Pro 3 )GIP does not improve its biological effectiveness as a GIP receptor antagonist.

Characterisation and glucoregulatory actions of a novel acylated form of the (Pro 3 )GIP receptor antagonist in type 2 diabetes