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dc.contributor.authorBabgi, Bandar A.
dc.contributor.authorAlsayari, Jalal
dc.contributor.authorAlenezi, Hana M.
dc.contributor.authorAbdellatif, Magda H.
dc.contributor.authorEltayeb, Naser E.
dc.contributor.authorEmwas, Abdul-Hamid M.
dc.contributor.authorJaremko, Mariusz
dc.contributor.authorHussien, Mostafa A.
dc.date.accessioned2021-03-29T10:38:14Z
dc.date.available2021-03-29T10:38:14Z
dc.date.issued2021-03-29
dc.identifier.citationBabgi, B. A., Alsayari, J., Alenezi, H. M., Abdellatif, M. H., Eltayeb, N. E., Emwas, A.-H. M., … Hussien, M. A. (2021). Alteration of Anticancer and Protein-Binding Properties of Gold(I) Alkynyl by Phenolic Schiff Bases Moieties. Pharmaceutics, 13(4), 461. doi:10.3390/pharmaceutics13040461
dc.identifier.issn1999-4923
dc.identifier.pmid33805337
dc.identifier.doi10.3390/pharmaceutics13040461
dc.identifier.urihttp://hdl.handle.net/10754/668359
dc.description.abstractA set of five gold complexes with the general formula Au(PR3)(C≡C-C6H4-4-R′) (R = PPh3, R′ = –CHO (1), R = PCy3, R′ = –CHO (2), R = PPh3, R′ = –N=CH-C6H4-2-OH (3), R = PPh3, R′ = –N=CH-C6H4-4-OH (4), R = PCy3, R′ = –N=CH-C6H4-2-OH (5)) were synthesized and characterized by elemental analysis, 1H-NMR spectroscopy, 31P-NMR spectroscopy, and mass spectrometry. The structures of complexes 2 and 5 were determined by X-ray crystallography. The effects of the structural modifications on the protein binding affinities and anticancer activities of the five gold complexes were assessed. Fluorescence quenching experiments to assess binding to human serum albumin (HSA) revealed that the Schiff base complexes (3, 4, and 5) had binding constants that were superior to their parent aldehyde complexes and highlighted the position of the hydroxy group because complex 4 (4-hydroxy) had a binding constant 6400 times higher than complex 3 (2-hydroxy). The anticancer activities of the complexes against the OVCAR-3 (ovarian carcinoma) and HOP-62 (non-small-cell lung) cancer cell lines showed that the Schiff bases (3–5) were more cytotoxic than the aldehyde-containing complexes (1 and 2). Notably, compound 4 had cytotoxic activity comparable to that of cisplatin against OVCAR-3, demonstrating the significance of the para position for the hydroxy group. Molecular docking studies against the enzyme thioredoxin reductase (TrxR) and human serum albumin were conducted, with docking scores in good agreement with the experimental data. The current study highlights how small structural modifications can alter physiochemical and anticancer properties. Moreover, this simple design strategy using the aldehyde group can generate extensive opportunities to explore new gold(I)-based anticancer drugs via condensation, cyclization, or nucleophilic addition reactions of the aldehyde.
dc.description.sponsorshipM.H.A. is very thankful for Taif University researcher support; project number: TURSP/91, Taif University, Taif, Saudi Arabia. M.J. would like to express his thanks to KAUST for financial and technical support. H.M.A. and B.A.B. would like to express their thanks to KACST for financially supporting this work.
dc.description.sponsorshipHana M. Alenezi would like to thank King Fahd Medical Research Centre (KFMRC) at KAU for allowing the use of their facilities. Mariusz Jaremko and Abdul-Hamid M. Emwas would like to thank the King Abdullah University of Science and Technology (KAUST) for the financial support. Magda H. Abdellatif is very thankful for Taif University researcher support; project number: TURSP/91, Taif University, Taif, Saudi Arabia.
dc.language.isoen
dc.publisherMDPI AG
dc.relation.urlhttps://www.mdpi.com/1999-4923/13/4/461
dc.rights© 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.titleAlteration of Anticancer and Protein-Binding Properties of Gold(I) Alkynyl by Phenolic Schiff Bases Moieties
dc.typeArticle
dc.contributor.departmentNMR
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.contributor.departmentBioscience Program
dc.identifier.journalPharmaceutics
dc.eprint.versionPublisher's Version/PDF
dc.contributor.institutionDepartment of Chemistry, Faculty of Science, King Abdulaziz University, P.O. Box 80203, Jeddah 21589, Saudi Arabia
dc.contributor.institutionChemistry Department, Deanship of Scientific Research, College of Sciences, Taif University, Al-Haweiah, P.O. Box 11099, Taif 21944, Saudi Arabia
dc.contributor.institutionDepartment of Chemistry, College of Science and Arts, King Abdulaziz University, P.O. Box 344, Rabigh 21911, Saudi Arabia
dc.contributor.institutionDepartment of Chemistry, Faculty of Science, Port Said University, Port Said 42521, Egypt
dc.identifier.volume13
dc.identifier.issue4
dc.contributor.affiliationKing Abdullah University of Science and Technology (KAUST)
dc.right.copyrightThis article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license.
dc.identifier.pages461
pubs.publication-statusPublished
kaust.personEmwas, Abdul-Hamid M.
kaust.personJaremko, Mariusz
dc.date.accepted2021-03-18
refterms.dateFOA2021-03-29T10:38:15Z


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© 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
Except where otherwise noted, this item's license is described as © 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).