Targeting the insulin receptor with hormone and peptide dimers
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15640%2F22%3A73618689" target="_blank" >RIV/61989592:15640/22:73618689 - isvavai.cz</a>
Alternative codes found
RIV/61388963:_____/23:00564527 RIV/00216208:11310/23:10464279
Result on the web
<a href="https://onlinelibrary.wiley.com/doi/10.1002/psc.3461" target="_blank" >https://onlinelibrary.wiley.com/doi/10.1002/psc.3461</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/psc.3461" target="_blank" >10.1002/psc.3461</a>
Alternative languages
Result language
angličtina
Original language name
Targeting the insulin receptor with hormone and peptide dimers
Original language description
Insulin is a key hormone involved in the regulation of overall energetic homeostasis of the organism. 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. Herewith, 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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
21002 - Nano-processes (applications on nano-scale); (biomaterials to be 2.9)
Result continuities
Project
<a href="/en/project/EF16_019%2F0000729" target="_blank" >EF16_019/0000729: Chemical biology for drugging undruggable targets</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2022
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
JOURNAL OF PEPTIDE SCIENCE
ISSN
1075-2617
e-ISSN
1099-1387
Volume of the periodical
29
Issue of the periodical within the volume
4
Country of publishing house
GB - UNITED KINGDOM
Number of pages
9
Pages from-to
"nečíslováno"
UT code for WoS article
000883179300001
EID of the result in the Scopus database
2-s2.0-85142158035