Protein–drug interactions are crucial for understanding drug delivery and cell functions. Jacalin is a suitable molecule for such targeting, as it specifically recognizes the tumor-associated Thomsen–Friedenreich (TF) antigen that is expressed on the glycosylated proteins in cancer cells. The present paper describes the interaction of curcumin and jacalin, a possible carrier molecule for the delivery of antitumor drugs due to its ability to recognize tumor cells. Our results have shown that both steady-state fluorescence and fluorescent labelling of jacalin are two reliable methods to determine jacalin-curcumin interactions. The affinity of jacalin for curcumin is consistently within the micromolar range (using fluorescence and microscale thermophoresis) showing high-affinity binding of the complex. In vitro experiments on triple-negative breast cancer MDA-MB-231 cells indicated inhibition of cell growth after treating with the jacalin-curcumin complex for 48 h. The cell survival fraction was significantly reduced to 50% after combined treatment. In this paper, we report for the first time about the jacalin-curcumin interaction. We quantified this unique biomolecular interaction and gathered additional information on the binding event. We observed that the jacalin-curcumin complex inhibits the proliferation of the triple-negative breast cancer MDA-MB-231 cells.

Recent studies have discovered that aryl-substituted pyrido[2,1-a]isoquinolines have the potential to be highly active DPP IV inhibitors. In previous studies, we reported a novel synthetic approach for the construction of their sulfur-containing bioisosteric [1,4]thiazino[3,4-a]isoquinolines analogues, incorporating an additional aryl substituent. The present study aims to investigate the DPP IV inhibitory activity and cytotoxicity of the synthesized molecules by in vitro assay. The geometry optimization and molecular docking of the synthesized compounds were used to determine their binding modes to the active site of DPP IV. The docking analysis revealed that the energy-minimized poses of the studied compounds are close to the most important selectivity cliffs for DPP IV inhibition, forming hydrogen bonds and hydrophobic interactions with them. These results can be considered as a preliminary step towards further structural activity modifications.

Protein-drug interactions are crucial for understanding drug delivery and cell functions. Jacalin is a suitable molecule for such targeting, as it specifically recognizes the tu-mor-associated Thomsen-Friedenreich antigen that is expressed on the glycosylated proteins in cancer cells. The present paper describes the interaction of curcumin and jacalin, a possible carrier molecule for the delivery of antitumor drugs due to its ability to recognize tumor cells. Our results have shown that both steady state fluorescence and fluorescent label-ling of jacalin are two reliable methods to determine jacalin-curcumin interactions. The affinity of jacalin for curcumin is consistently within the micromolar range (using flu-orescence and microscale thermophoresis) showing high-affinity binding of the com-plex. In vitro experiments on the triple negative breast cancer MDA-MB-231 cells indi-cated inhibition of cell growth after treating with the jacalin-curcumin complex for 48 h. The cell survival fraction was significantly reduced to 50% after combined treatment. In this paper, we report for the first time about the jacalin-curcumin interaction. We quantified this unique biomolecular interaction and gathered additional information on the binding event. We observed that the jacalin-curcumin complex inhibits the proliferation of the triple negative breast cancer MDA-MB-231 cells.

Prostate cancer is one of the leading causes of death among men. Our study focuses on seeking new compounds and combinations to diminish the severe side effects of classical anticancer drugs for treating this type of cancer. In this study, we investigated and compared the classical anticancer drug docetaxel and non-classical compounds, Au porphyrin, and the plant lectin jacalin, and in different combinations on the prostate cancer cell line PC3. Jacalin, isolated from jackfruit seeds by affinity chromatography on immobilized galactose, specifically recognizes the tumor-associated Thomsen–Friedenreich antigen. The present investigation shows the interaction of jacalin with Au porphyrin, registering conformational changes within the protein due to the binding. From the titration curve, the affinity of 1.8 ± 0.39 µM for the jacalin—Au porphyrin complex was calculated. In vitro experiments with PC3 cells treated with docetaxel, Au porphyrin, jacalin and combinations indicated a decrease in cell viability. The IC₅₀ for Au porphyrin and for docetaxel were studied and indicated that the calculated IC₅₀ for docetaxel was 8 orders of magnitude higher than that for Au porphyrin. Interestingly, we found that jacalin-Au porphyrin complex is more cytotoxic reaching cell viability of 34%, than docetaxel-Au-porphyrin complex (with cell viability above 50%). Our results demonstrate the effects of three compounds as well as the effects of their combinations upon PC3 cells. Interestingly, low concentrations of the plant lectin jacalin (3 µM) facilitated the cell cytotoxicity of Au-porphyrin, showing new perspectives in cancer treatment.