Human insulin A-chain peptide analog(s) with in vitro biological activity.

In a previous study, we showed that a synthetic human insulin 1-chain analog, named analog (3) was capable of mimicking in vitro effects of native insulin, including stimulation of cell proliferation, glucose uptake and glycogen synthesis. Here, we have synthesized three new analogs (6, 9, 12) of the human A-chain, bearing or not their N- or C-terminal residue, to determine the structural features which are responsible for their biological properties. In vitro experiments clearly demonstrated that the N-terminal part of the peptides is required for the biological activity of the molecules, suggesting its crucial role in the mechanism underlying the cellular effect.