Počet záznamů: 1
Targeting the insulin receptor with hormone and peptide dimers
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SYSNO ASEP 0564527 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Targeting the insulin receptor with hormone and peptide dimers Tvůrce(i) Lin, Jingjing (UOCHB-X)
Selicharová, Irena (UOCHB-X) RID, ORCID
Mitrová, Katarína (UOCHB-X)
Fabre, Benjamin (UOCHB-X) ORCID
Miriyala, Vijay Madhav (UOCHB-X)
Lepšík, Martin (UOCHB-X) RID, ORCID
Jiráček, Jiří (UOCHB-X) RID, ORCID
Garre Hernández, María Soledad (UOCHB-X) ORCIDČíslo článku e3461 Zdroj.dok. Journal of Peptide Science - ISSN 1075-2617
Roč. 29, č. 4 (2023)Poč.str. 9 s. Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova insulin ; dimer ; bioconjugate ; agonism ; antagonism ; peptidomimetics ; receptor ; peptide hormone Obor OECD Biochemistry and molecular biology CEP EF16_019/0000729 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy Způsob publikování Omezený přístup Institucionální podpora UOCHB-X - RVO:61388963 UT WOS 000883179300001 EID SCOPUS 85142158035 DOI 10.1002/psc.3461 Anotace The dimeric character of the receptor for insulin evokes ideas about its activation or inhibition with peptide dimers that could either trigger or block the structural transition of the insulin receptor, leading to its activation. We present the chemical engineering and biological characterization of several series of insulin dimers or dimers of specific peptides that should be able to bind receptors for insulin or insulin growth factor 1. The hormones or peptides in the dimers were interconnected with different linkers, consisting of triazole moieties and 3, 6, 8, 11, or 23 polyethylene glycol units. The prepared dimers were weaker in binding to insulin receptors than human insulin. However, some of the insulin dimers showed preferential binding specificity toward the isoform A of the insulin receptor, and the insulin dimers also stimulated the insulin receptor more strongly than would be consistent with their binding affinities. Our results suggest that designing insulin dimers may be a promising strategy for modulating the ability of the hormone to activate the receptor or to alter its specificity toward insulin receptor isoforms. Pracoviště Ústav organické chemie a biochemie Kontakt asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Jana Procházková, Tel.: 220 183 418 Rok sběru 2024 Elektronická adresa https://doi.org/10.1002/psc.3461
Počet záznamů: 1