Search for New Aggregable Fragments of Human Insulin
| Autor: | Slawomir Wiak, Monika Swiontek, Joanna Wasko, Agata Chaberska, Lukasz Pietrzak, Zbigniew J. Kaminski, Beata Kolesinska, Justyna Fraczyk, Lukasz Szymanski |
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| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
Circular dichroism
amyloid deposits medicine.medical_treatment Pharmaceutical Science triazine coupling reagents Article Analytical Chemistry lcsh:QD241-441 Protein Aggregates Aggregation SPPS lcsh:Organic chemistry Drug Discovery medicine Human insulin Humans Insulin Amino Acid Sequence Physical and Theoretical Chemistry Conformational isomerism Solid-Phase Synthesis Techniques diabetes Chemistry Triazines Organic Chemistry Coupling reagent Peptide Fragments Solutions Kinetics Chemistry (miscellaneous) amyloid-like fiber formation Biophysics Molecular Medicine Thermodynamics Indicators and Reagents Oligopeptides |
| Zdroj: | Molecules Volume 24 Issue 8 Molecules, Vol 24, Iss 8, p 1600 (2019) |
| ISSN: | 1420-3049 |
| DOI: | 10.3390/molecules24081600 |
| Popis: | In this study, three independent methods were used to identify short fragment of both chains of human insulin which are prone for aggregation. In addition, circular dichroism (CD) research was conducted to understand the progress of aggregation over time. The insulin fragments (deca- and pepta-peptides) were obtained by solid-phase synthesis using 4-(4,6-dimethoxy-1,3,5-triazin-2-yl)-4-methylmorpholinium toluene-4-sulfonate (DMT/NMM/TosO-) as a coupling reagent. Systematic studies allowed identification of the new fragments, expected to be engaged in triggering aggregation of the entire structure of human insulin under physiological conditions. It was found that the aggregation process occurs through various structural conformers and may favor the formation of a fibrous structure of aggregate. |
| Databáze: | OpenAIRE |
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