preprints.org > biology and life sciences > biochemistry and molecular biology > doi: 10.20944/preprints202311.1583.v1

Preprint Communication Version 1 Preserved in Portico This version is not peer-reviewed

Version 1 : Received: 24 November 2023 / Approved: 24 November 2023 / Online: 26 November 2023 (06:30:33 CET)

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.

Protein-ligand interaction; Curcumin; Jacalin; Lectin; Fluorescence; Cytotoxicity; Breast cancer cells; MDA-MB-231

Biology and Life Sciences, Biochemistry and Molecular Biology

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