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Targeting nucleolin by RNA G-quadruplex-forming motif
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SYSNO ASEP 0554897 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Targeting nucleolin by RNA G-quadruplex-forming motif Author(s) Figueiredo, J. (PT)
Miranda, A.I. (PT)
Lopes-Nunes, J. (PT)
Carvalho, J. (PT)
Alexandre, D. (PT)
Valente, S. (PT)
Mergny, Jean-Louis (BFU-R) ORCID, RID
Cruz, C. (PT)Number of authors 8 Article number 114418 Source Title Biochemical Pharmacology. - : Elsevier - ISSN 0006-2952
Roč. 189, JUL 2021 (2021)Number of pages 11 s. Publication form Online - E Language eng - English Country US - United States Keywords cell lung-cancer ; expression ; micrornas ; pre-MIR150 G-quadruplex forming sequence ; Nucleolin OECD category Pharmacology and pharmacy R&D Projects EF15_003/0000477 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Method of publishing Limited access Institutional support BFU-R - RVO:68081707 UT WOS 000662575900004 EID SCOPUS 85099863465 DOI 10.1016/j.bcp.2021.114418 Annotation A high level of nucleolin (NCL) expression is often associated with a poor prognosis of patients with lung cancer (LC), suggesting that NCL can be used as a possible biomarker. NCL has been shown to display a marked preference for the binding to G-quadruplexes (G4). Here, we investigate the formation of an RNA quadruplex structure in a sequence found in the human precursor pre-MIR150 with the potential to recognize NCL. Circular dichroism (CD) spectra of pre-MIR150 G4forming sequence (designated by rG4) indicate the formation of a parallel quadruplex structure in KCl or when complexed with the well-known G4 ligand PhenDC3. The thermal stability of rG4 is very high, and further increases in the presence of PhenDC3. The binding affinities of rG4 to PhenDC3 and NCL RBD1,2 are similar with KD values in the nanomolar range. PAGE results suggest the formation of a ternary quadruplex-ligand-protein complex (rG4-PhenDC3-NCL RBD1,2), indicative that PhenDC3 does not prevent the binding of rG4 to NCL RBD1,2. Finally, rG4 can recognize NCL-positive cells and, when fluorescently labeled, can be used as a probe for this protein. ELISA experiments indicate altered NCL expression patterns in liquid biopsies of LC patients in a non-invasive manner, potentially helping the diagnosis, prognosis, and patient response to treatment. Hence, labeled rG4 could be used as a detection probe of LC in liquid biopsies. Workplace Institute of Biophysics Contact Jana Poláková, polakova@ibp.cz, Tel.: 541 517 244 Year of Publishing 2022 Electronic address https://www.sciencedirect.com/science/article/pii/S0006295221000149?via%3Dihub
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