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Updated: Jun 13, 2026

Homogeneous Time-resolved Förster Resonance Energy Transfer-based Assay for Detection of Insulin Secretion
Published on: May 10, 2018
Aspartimide modified galanin analogue antagonizes galanin action on insulin secretion
Jarosław Ruczyński1, Zdzisław Konstański, Magdalena Cybal
1Department of Chemistry, University of Gdańsk, Sobieskiego 18, 80-952 Gdańsk, Poland. ruczynski@chem.univ.gda.pl
Abstract:
Aspartimide (Asi) formation is one of the most serious side reactions that can occur both during solid phase synthesis and storage of peptides containing aspartic acid. Although numerous studies on the mechanism of Asi formation conducted so far, the problem still remains unresolved and relatively little is known about the impact of this side reaction on biological properties of such modified peptides. In the present work we characterized the effect of Asi formation on biological properties of galanin(1-15) analogue modified in position 14 with aspartic acid, investigating its action on rat isolated gastric smooth muscles and glucose-induced insulin secretion from rat isolated islets of Langerhans. Our results show that this side process may adversely affect biological properties of such modified peptides. As we expected, modification of GAL(1-15)NH(2) structure changed the interaction of GAL(1-15)NH(2) with its receptors and consequently yielded peptide which, in studies on insulin secretion, showed insulinotropic- and antagonistic activities as compared to Asi-free analogue.
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