Bombesin, bombesin analogs, and related peptides: effects on thermoregulation

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Abstract
The synthesis and biological evaluation on thermoregulation of 39 peptides related to bombesin (structural analogs or other naturally occurring peptides) were described. The bioassay system reported measures the ability of peptides injected intracisternally to lower body temperature of cold(4.degree. C)-exposed rats. The most potent bombesin analogs were those in which positions 1-5 (not included) were altered, indicating that the decapeptide C terminal was sufficient for full potency. Gln at the 7th position and Gly at the 11th position were replaced by D-Gln and D-Ala (but not D-Pro or D-Phe), respectively, without any change in potency. Methionine at the 14 position was replaced with its D isomer with retention of 10% biological activity. Any other alteration of the C terminus (deletions or free acid, with the exception of the N-methylamide) drastically reduced the biological potency of those peptides. Among other naturally occurring peptides, alytesin had 100% of bombesin potency but litorin, neurotensin, xenopsin, substance P, physalaemin and eledoisin were in the order of 104 times less potent. The shortest peptide which had full biological activity was the octapepetide des-Glp-Gln-Arg-Leu-Gly-Asn[D-Glp7,D-Ala11]-bombesin.

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