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Pseudin-2 is a cationic α-helical peptide that was first isolated from the skin of the paradoxical frog  Pseudis paradoxa  on the basis of its antimicrobial activity. We have investigated the insulin-releasing properties and cytotoxicity of the peptide, together with selected analogues with increased cationicity and hydrophobicity. At concentrations in the range 10 -9 –10 -6   m , pseudin-2, and its [Lys 18 ], [Phe 8 ], and [ d -Lys 3 , d -Lys 10 , d -Lys 14 ] derivatives, stimulated insulin release from the BRIN-BD11 clonal β-cell line without increasing release of lactate dehydrogenase. The [Lys 18 ] analogue was the most potent (46% increase in insulin release at 10 -9   m ) and the most effective (215% increase in insulin release at 10 -6   m ). The more cationic [Lys 3 ,Lys 10 ,Lys 14 ] and [Lys 3 ,Lys 10 ,Lys 14 ,Lys 21 ] analogues lacked insulinotropic action and the more hydrophobic [Phe 16 ] analogue was cytotoxic at concentrations ≥10 -7   m . Pseudin-2 and [Lys 18 ]-pseudin-2 had no effect on intracellular calcium concentrations and stimulated insulin release in the absence of external calcium. [Lys 18 ]-pseudin-2 (10 -8   m ) stimulated insulin release in the presence of diazoxide and verapamil. Our results demonstrate that pseudin-2 stimulates insulin secretion from BRIN-BD11 cells by a mechanism involving Ca 2+ -independent pathways and identify [Lys 18 ]-pseudin-2 as a peptide that may have potential for development as a therapeutically valuable insulinotropic agent for the treatment of type 2 diabetes.

Insulin-releasing properties of the frog skin peptide pseudin-2 and its [Lys 18 ]-substituted analogue