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https://doi.org/10.3390/ijms10125398
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Campo DC | Valor | Lengua/Idioma |
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dc.contributor.author | Sánchez del Campo Ferrer, Luis | - |
dc.contributor.author | Sáez Ayala, Magalí | - |
dc.contributor.author | Chazarra Parres, Soledad | - |
dc.contributor.author | Cabezas Herrera, Juan | - |
dc.contributor.author | Rodríguez López, José Neptuno | - |
dc.contributor.other | Facultades, Departamentos, Servicios y Escuelas::Departamentos de la UMU::Bioquímica y Biología Molecular A | es |
dc.date.accessioned | 2024-01-02T12:37:51Z | - |
dc.date.available | 2024-01-02T12:37:51Z | - |
dc.date.issued | 2009-12-18 | - |
dc.identifier.citation | International Journal of Molecular Sciences. Volumen 10. nº12. Páginas 5398-5410 | es |
dc.identifier.issn | 1422-0067 | - |
dc.identifier.uri | http://hdl.handle.net/10201/136986 | - |
dc.description | This is a Published version of the following article, in International Journal of Molecular Sciences. https://doi.org/10.3390/ijms10125398]. It is deposited under the terms of the Creative Commons Attribution-Non Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial reuse, distribution, and reproduction in any medium, provided the original work is properly cited. | es |
dc.description.abstract | Dihydrofolate reductase (DHFR) is the subject of intensive investigation since it appears to be the primary target enzyme for antifolate drugs. Fluorescence quenching experiments show that the ester bond-containing tea polyphenols (-)-epigallocatechin gallate (EGCG) and (-)-epicatechin gallate (ECG) are potent inhibitors of DHFR with dissociation constants (K-D) of 0.9 and 1.8 mu M, respectively, while polyphenols lacking the ester bound gallate moiety [e.g., (-)-epigallocatechin (EGC) and (-)-epicatechin (EC)] did not bind to this enzyme. To avoid stability and bioavailability problems associated with tea catechins we synthesized a methylated derivative of ECG (3-O-(3,4,5-trimethoxybenzoyl)(-)-epicatechin; TMECG), which effectively binds to DHFR (K-D = 2.1 mu M). In alkaline solution, TMECG generates a stable quinone methide product that strongly binds to the enzyme with a K-D of 8.2 nM. Quercetin glucuronides also bind to DHFR but its effective binding was highly dependent of the sugar residue, with quercetin-3-xyloside being the stronger inhibitor of the enzyme with a K-D of 0.6 mu M. The finding that natural polyphenols are good inhibitors of human DHFR could explain the epidemiological data on their prophylactic effects for certain forms of cancer and open a possibility for the use of natural and synthetic polyphenols in cancer chemotherapy. | es |
dc.format | application/pdf | es |
dc.format.extent | 13 | es |
dc.language | eng | es |
dc.publisher | MDPI | es |
dc.relation | Ámbito del proyecto: Regional. Agencia financiadora: Fundación Séneca (CARM) Código o número del acuerdo de subvención: 08595/PI/08 | es |
dc.rights | info:eu-repo/semantics/openAccess | es |
dc.rights | Atribución 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | * |
dc.subject | Polyphenols | es |
dc.subject | Tea catechins | es |
dc.subject | Flavonoids | es |
dc.subject | Dihydrofolate reductase | es |
dc.subject | Antifolates | es |
dc.subject | Enzyme inhibition | es |
dc.subject.other | CDU::5 - Ciencias puras y naturales::57 - Biología::577 - Bioquímica. Biología molecular. Biofísica | es |
dc.title | Binding of Natural and Synthetic Polyphenols to Human Dihydrofolate Reductase | es |
dc.type | info:eu-repo/semantics/article | es |
dc.identifier.doi | https://doi.org/10.3390/ijms10125398 | - |
Aparece en las colecciones: | Artículos: Bioquímica y Biología Molecular "A" |
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