Study summary · research use only
Stapled Vasoactive Intestinal Peptide (VIP) Derivatives Improve VPAC2 Agonism and Glucose-Dependent Insulin Secretion
Plain-language summary
Paraphrased from the published abstract below — not a verdict on whether anything works.
In this study, the authors investigated two peptide cyclization strategies, lactamisation and olefin-metathesis stapling, applied to vasoactive intestinal peptide (VIP), an agonist of VIP receptor 2 (VPAC2), and their effects on VPAC2 agonism, secondary structure, protease stability, and cell membrane permeability. The abstract reports that some VIP analogues showed enhanced VPAC2 agonist potency, glucose-dependent insulin secretion activity, and increased helical content, but that neither cyclization strategy appeared to affect proteolytic stability or cell permeability of the resulting peptides.
Abstract
Agonists of vasoactive intestinal peptide receptor 2 (VPAC2) stimulate glucose-dependent insulin secretion, making them attractive candidates for the treatment of hyperglycaemia and type-II diabetes. Vasoactive intestinal peptide (VIP) is an endogenous peptide hormone that potently agonizes VPAC2. However, VIP has a short serum half-life and poor pharmacokinetics in vivo and is susceptible to proteolytic degradation, making its development as a therapeutic agent challenging. Here, we investigated two peptide cyclization strategies, lactamisation and olefin-metathesis stapling, and their effects on VPAC2 agonism, peptide secondary structure, protease stability, and cell membrane permeability. VIP analogues showing significantly enhanced VPAC2 agonist potency, glucose-dependent insulin secretion activity, and increased helical content were discovered; however, neither cyclization strategy appeared to effect proteolytic stability or cell permeability of the resulting peptides.
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