Insulin Hot-Spot Analogs Formed with -Methylated Amino Acid Residues Inhibit Aggregation of Native Hormone.

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ID: 64049
2019
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Abstract
In this study, -methylated analogs of hot-spots of insulin were designed and synthesized, in the expectation that they would inhibit the aggregation of both insulin hot-spots and the entire hormone. Synthesis of insulin "amyloidogenic" analogs containing -methylated amino acid residues was performed by microwave-assisted solid phase according to the Fmoc/tert-Bu strategy. As a coupling reagent 4-(4,6-dimethoxy-1,3,5-triazin-2-yl)-4-methylmorpholinium toluene-4-sulfonate (DMT/NMM/TosO) was used. Three independent methods were applied in aggregation studies of the complexes of insulin with its -methylated peptides. Additionally, circular dichroism (CD) measurements were used to confirm that aggregation processes did not occur in the presence of the -methylated analogs of hot-spot insulin fragments, and that insulin retains its native conformation. Of the seven -methylated analogs of the A- and B-chain hot-spots of insulin, six inhibited insulin aggregation (peptides and -). All tested peptides were found to have a lower ability to inhibit the aggregation of insulin hot-spots compared to the capability to inhibit native hormone aggregation.
Reference Key
swiontek2019insulinmolecules Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Swiontek, Monika;Wasko, Joanna;Fraczyk, Justyna;Galecki, Krystian;Kaminski, Zbigniew J;Kolesinska, Beata;
Journal molecules
Year 2019
DOI
E3706
URL
Keywords
aggregation n-methylated analogs of insulin hot-spots inhibition of insulin aggregation microwave-assisted solid-phase peptide synthesis triazine coupling reagent

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