Background: Glucagon-like peptide-1 (GLP-1), glucose-dependent insulinotropic polypeptide (GIP), and glucagon have important gluco-regulatory actions. Results: Fusion of amino acid sequences of GLP-1, GIP, and glucagon produces hybrid peptides with triple-acting agonist activity. Conclusion: Hybrid peptides possess beneficial biological actions equivalent, or superior to, activation of single receptors. Significance: Multitargeting peptides offer a new class of therapeutics for obesity and diabetes.

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Glutamine (gln)-modified analogues of xenin may represent an attractive therapeutic approach for type 2 diabetes.

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Crude venom from two elapid snakes Pseudechis australis and Pseudechis butleri was fractionated by gel filtration chromatography and selected fractions screened for in vitro insulin-releasing activity using clonal pancreatic BRIN-BD11 cells. Following acute 20-min incubation at 5.6 mM glucose, 9 fractions exhibited significant (P < 0.001) insulin-releasing activity. Structural characterisation of active fractions was achieved primarily using MALDI-TOF MS and N-terminal Edman degradation sequencing. The partial N-terminal sequences are reported for a total of 7 venom components. Their homology to existing sequences as determined using BLAST searching uncovered the main insulin-releasing families as being phospholipases A2 and short α-neurotoxins. A number of sequences are reported for the first time from Pseudechis butleri venom which is much less studied than the related Pseudechis australis.