Search for New Aggregable Fragments of Human Insulin
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-pepti...
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doaj-9ac252dcb72a455e8ccc4c970c2c8a742020-11-24T22:19:07ZengMDPI AGMolecules1420-30492019-04-01248160010.3390/molecules24081600molecules24081600Search for New Aggregable Fragments of Human InsulinMonika Swiontek0Justyna Fraczyk1Joanna Wasko2Agata Chaberska3Lukasz Pietrzak4Zbigniew J. Kaminski5Lukasz Szymanski6Slawomir Wiak7Beata Kolesinska8Institute of Organic Chemistry, Lodz University of Technology, Zeromskiego 116, 90-924 Lodz, PolandInstitute of Organic Chemistry, Lodz University of Technology, Zeromskiego 116, 90-924 Lodz, PolandInstitute of Organic Chemistry, Lodz University of Technology, Zeromskiego 116, 90-924 Lodz, PolandInstitute of Organic Chemistry, Lodz University of Technology, Zeromskiego 116, 90-924 Lodz, PolandInstitute of Mechatronics and Information Systems, Faculty of Electrical, Electronic, Computer and Control Engineering, Lodz University of Technology, Stefanowskiego 18/22, 90-924 Lodz, PolandInstitute of Organic Chemistry, Lodz University of Technology, Zeromskiego 116, 90-924 Lodz, PolandInstitute of Mechatronics and Information Systems, Faculty of Electrical, Electronic, Computer and Control Engineering, Lodz University of Technology, Stefanowskiego 18/22, 90-924 Lodz, PolandInstitute of Mechatronics and Information Systems, Faculty of Electrical, Electronic, Computer and Control Engineering, Lodz University of Technology, Stefanowskiego 18/22, 90-924 Lodz, PolandInstitute of Organic Chemistry, Lodz University of Technology, Zeromskiego 116, 90-924 Lodz, PolandIn 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<sup>-</sup>) 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.https://www.mdpi.com/1420-3049/24/8/1600Aggregationamyloid depositsamyloid-like fiber formationdiabetesSPPStriazine coupling reagents |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Monika Swiontek Justyna Fraczyk Joanna Wasko Agata Chaberska Lukasz Pietrzak Zbigniew J. Kaminski Lukasz Szymanski Slawomir Wiak Beata Kolesinska |
spellingShingle |
Monika Swiontek Justyna Fraczyk Joanna Wasko Agata Chaberska Lukasz Pietrzak Zbigniew J. Kaminski Lukasz Szymanski Slawomir Wiak Beata Kolesinska Search for New Aggregable Fragments of Human Insulin Molecules Aggregation amyloid deposits amyloid-like fiber formation diabetes SPPS triazine coupling reagents |
author_facet |
Monika Swiontek Justyna Fraczyk Joanna Wasko Agata Chaberska Lukasz Pietrzak Zbigniew J. Kaminski Lukasz Szymanski Slawomir Wiak Beata Kolesinska |
author_sort |
Monika Swiontek |
title |
Search for New Aggregable Fragments of Human Insulin |
title_short |
Search for New Aggregable Fragments of Human Insulin |
title_full |
Search for New Aggregable Fragments of Human Insulin |
title_fullStr |
Search for New Aggregable Fragments of Human Insulin |
title_full_unstemmed |
Search for New Aggregable Fragments of Human Insulin |
title_sort |
search for new aggregable fragments of human insulin |
publisher |
MDPI AG |
series |
Molecules |
issn |
1420-3049 |
publishDate |
2019-04-01 |
description |
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<sup>-</sup>) 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. |
topic |
Aggregation amyloid deposits amyloid-like fiber formation diabetes SPPS triazine coupling reagents |
url |
https://www.mdpi.com/1420-3049/24/8/1600 |
work_keys_str_mv |
AT monikaswiontek searchfornewaggregablefragmentsofhumaninsulin AT justynafraczyk searchfornewaggregablefragmentsofhumaninsulin AT joannawasko searchfornewaggregablefragmentsofhumaninsulin AT agatachaberska searchfornewaggregablefragmentsofhumaninsulin AT lukaszpietrzak searchfornewaggregablefragmentsofhumaninsulin AT zbigniewjkaminski searchfornewaggregablefragmentsofhumaninsulin AT lukaszszymanski searchfornewaggregablefragmentsofhumaninsulin AT slawomirwiak searchfornewaggregablefragmentsofhumaninsulin AT beatakolesinska searchfornewaggregablefragmentsofhumaninsulin |
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1725779994406289408 |