Synthesis of biologically active tritiated amylin and salmon calcitonin analogues

M. Heller, K. M. Loomes, G. J S Cooper

Research output: Contribution to journalArticlepeer-review

Abstract

Amylin is a hormone belonging to the calcitonin protein family of peptides. To facilitate receptor screening studies, alternatively radiolabeled and biologically active amylin and salmon calcitonin analogues were synthesized by reductive methylation. Free amino groups of amylin and salmon calcitonin were methylated by reaction of peptides with formaldehyde and sodium [3H]borohydride. Radioactively labeled peptides were purified by size exclusion chromatography followed by HPLC. Analysis by MALDI-TOF mass spectrometry of purified amylin and salmon calcitonin peptides revealed incorporation of both two and four tritiated methyl groups per peptide molecule. Specific activities of 22.6 and 23.2 GBq/mmol were measured for amylin and salmon calcitonin, respectively. Methylation of rat amylin and salmon calcitonin did not affect their biological activities as both retained their potency to inhibit insulin-stimulated glycogen synthesis in isolated rat soleus muscle. The synthesis of these tritiated analogues provides an alternative chemically stable radiolabeled ligand which may be useful in exploring receptor interactions within the calcitonin peptide family. (C) 2000 Academic Press.
Original languageEnglish
Pages (from-to)100-104
Number of pages4
JournalAnalytical Biochemistry
Volume285
Issue number1
DOIs
Publication statusPublished - 1 Oct 2000

Keywords

  • Amylin
  • Insulin resistance
  • Receptor binding
  • Type 2 diabetes

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