AI Article Synopsis
- The study builds on previous research that showed a synthetic insulin analog (3) can mimic native insulin's effects on cell growth and glucose metabolism.
- New analogs (6, 9, 12) were synthesized to explore which structural features influence their biological activity, revealing that the N-terminal part of these peptides is essential for their effectiveness.
- The findings suggest these mini-insulin variants derived from the A-chain could lead to new treatment strategies for diabetes, possibly offering advantages over traditional insulin.
Article Abstract
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. Our findings may help to better understand the mechanism of interaction between insulin and its receptor. In addition, the present data demonstrate that some mini-insulin derived from the A-chain can exert similar effects as native insulin. These small peptides may offer specific advantages over insulin in the definition of new strategies for diabetes treatment.
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| http://dx.doi.org/10.1002/cbf.1584 | DOI Listing |
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