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Functional stapled fragments of human preptin of minimised length
- 1.0556184 - ÚOCHB 2023 RIV GB eng J - Journal Article
Lubos, Marta - Mrázková, Lucie - Gwozdiaková, Petra - Pícha, Jan - Buděšínský, Miloš - Jiráček, Jiří - Kaminský, Jakub - Žáková, Lenka
Functional stapled fragments of human preptin of minimised length.
Organic & Biomolecular Chemistry. Roč. 20, č. 12 (2022), s. 2446-2454. ISSN 1477-0520. E-ISSN 1477-0539
R&D Projects: GA ČR(CZ) GA19-14069S; GA MŠMT(CZ) EF16_019/0000729; GA MŠMT LTAUSA18085
Research Infrastructure: e-INFRA CZ - 90140
Institutional support: RVO:61388963
Keywords : alpha-helical peptides * secondary structure * force field
OECD category: Biochemistry and molecular biology
Impact factor: 3.2, year: 2022
Method of publishing: Limited access
https://doi.org/10.1039/D1OB02193A
Preptin is peptide derived from the of insulin-like growth factor 2 ( pro-IGF2). We describe the synthesis, structures, and biological activities of scyclic analogues of human preptin with different covalent intramolecular bridges. We monitored the secondary structures of the stapled peptides using circular dichroism. The biological effect of the structural changes was determined afterwards by the ability of peptides to stimulate the release of intracellular calcium ions. Our findings could open up new ways to design new preptin analogues, which may have potential as drugs for the treatment of diabetes and osteoporosis.
Permanent Link: http://hdl.handle.net/11104/0331047
Number of the records: 1