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Synergistic Inhibitory Effect of Quercetin and Cyanidin-3O-Sophoroside on ABCB1.
Singh, Kuljeet; Patil, Rajesh B; Patel, Vikas; Remenyik, Judit; Hegedus, Tamás; Goda, Katalin.
Affiliation
  • Singh K; Department of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.
  • Patil RB; Doctoral School of Molecular Cell and Immune Biology, University of Debrecen, 4032 Debrecen, Hungary.
  • Patel V; Department of Pharmaceutical Chemistry, Sinhgad Technical Education Society's Sinhgad College of Pharmacy, OffSinhgad Road, Vadgaon (Bk), Pune 411041, Maharashtra, India.
  • Remenyik J; Department of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.
  • Hegedus T; Institute of Food Technology, Faculty of Agricultural and Food Sciences and Environmental Management, University of Debrecen, 4032 Debrecen, Hungary.
  • Goda K; Department of Biophysics and Radiation Biology, Semmelweis University, 1085 Budapest, Hungary.
Int J Mol Sci ; 24(14)2023 Jul 12.
Article in En | MEDLINE | ID: mdl-37511101
The human ABCB1 (P-glycoprotein, Pgp) protein is an active exporter expressed in the plasma membrane of cells forming biological barriers. In accordance with its broad substrate spectrum and tissue expression pattern, it affects the pharmacokinetics of numerous chemotherapeutic drugs and it is involved in unwanted drug-drug interactions leading to side effects or toxicities. When expressed in tumor tissues, it contributes to the development of chemotherapy resistance in malignancies. Therefore, the understanding of the molecular details of the ligand-ABCB1 interactions is of crucial importance. In a previous study, we found that quercetin (QUR) hampers both the transport and ATPase activity of ABCB1, while cyandin-3O-sophroside (C3S) stimulates the ATPase activity and causes only a weak inhibition of substrate transport. In the current study, when QUR and C3S were applied together, both a stronger ATPase inhibition and a robust decrease in substrate transport were observed, supporting their synergistic ABCB1 inhibitory effect. Similar to cyclosporine A, a potent ABCB1 inhibitor, co-treatment with QUR and C3S shifted the conformational equilibrium to the "inward-facing" conformer of ABCB1, as it was detected by the conformation-selective UIC2 mAb. To gain deeper insight into the molecular details of ligand-ABCB1 interactions, molecular docking experiments and MD simulations were also carried out. Our in silico studies support that QUR and C3S can bind simultaneously to ABCB1. The most favourable ligand-ABCB1 interaction is obtained when C3S binds to the central substrate binding site and QUR occupies the "access tunnel". Our results also highlight that the strong ABCB1 inhibitory effect of the combined treatment with QUR and C3S may be exploited in chemotherapy protocols for the treatment of multidrug-resistant tumors or for improving drug delivery through pharmacological barriers.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Quercetin / ATP Binding Cassette Transporter, Subfamily B / Antineoplastic Agents Type of study: Guideline Limits: Humans Language: En Journal: Int J Mol Sci Year: 2023 Document type: Article Affiliation country: Hungary Country of publication: Switzerland

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Quercetin / ATP Binding Cassette Transporter, Subfamily B / Antineoplastic Agents Type of study: Guideline Limits: Humans Language: En Journal: Int J Mol Sci Year: 2023 Document type: Article Affiliation country: Hungary Country of publication: Switzerland