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7 results on '"Kolesinska, Beata"'

1. Synthesis and Hemostatic Activity of New Amide Derivatives

Author

Banach, Lukasz, primary, Janczewski, Lukasz, additional, Kajdanek, Jakub, additional, Milowska, Katarzyna, additional, Kolodziejczyk-Czepas, Joanna, additional, Galita, Grzegorz, additional, Rozpedek-Kaminska, Wioletta, additional, Kucharska, Ewa, additional, Majsterek, Ireneusz, additional, and Kolesinska, Beata, additional

Published
2022
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4. Search for New Aggregable Fragments of Human Insulin

Author

Swiontek, Monika, primary, Fraczyk, Justyna, additional, Wasko, Joanna, additional, Chaberska, Agata, additional, Pietrzak, Lukasz, additional, Kaminski, Zbigniew J., additional, Szymanski, Lukasz, additional, Wiak, Slawomir, additional, and Kolesinska, Beata, additional

Published
2019
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6. Search for Fibrous Aggregates Potentially Useful in Regenerative Medicine Formed under Physiological Conditions by Self-Assembling Short Peptides Containing Two Identical Aromatic Amino Acid Residues

Author

Fraczyk, Justyna, primary, Lipinski, Wojciech, additional, Chaberska, Agata, additional, Wasko, Joanna, additional, Rozniakowski, Kamil, additional, Kaminski, Zbigniew, additional, Bogun, Maciej, additional, Draczynski, Zbigniew, additional, Menaszek, Elzbieta, additional, Stodolak-Zych, Ewa, additional, Kaminska, Marta, additional, and Kolesinska, Beata, additional

Published
2018
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7. Insulin Hot-Spot Analogs Formed with N-Methylated Amino Acid Residues Inhibit Aggregation of Native Hormone.

Author

Swiontek, Monika, Wasko, Joanna, Fraczyk, Justyna, Galecki, Krystian, Kaminski, Zbigniew J., and Kolesinska, Beata

Subjects
AMINO acid residues, INSULIN derivatives, INSULIN synthesis, HORMONES, PEPTIDE hormones, PEPTIDES
Abstract

In this study, N-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 N-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 N-methylated peptides. Additionally, circular dichroism (CD) measurements were used to confirm that aggregation processes did not occur in the presence of the N-methylated analogs of hot-spot insulin fragments, and that insulin retains its native conformation. Of the seven N-methylated analogs of the A- and B-chain hot-spots of insulin, six inhibited insulin aggregation (peptides 1 and 3–7). 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. [ABSTRACT FROM AUTHOR]

Published
2019
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