Isolation of banana lectin from Musa paradisiaca and investigation of its interactions with selected anticancer drugs: Insights from spectroscopic, computational and cellular studies.

BACKGROUND

Banana lectin (Banlec), a mannose/glucose-specific lectin isolated from Musa paradisiaca, is known for its immunomodulatory, antiviral and anticancer properties. However, its molecular interactions with anticancer drugs remain insufficiently explored, limiting its translational potential in targeted drug delivery.

OBJECTIVES

This study aimed to purify Banlec and systematically investigate its binding interactions with selected FDA-approved anticancer drugs, dasatinib, 5-fluorouracil (5-FU) and anastrozole, to gain mechanistic insights into Banlec-drug recognition and stability.

METHODS

Banlec was purified from ripened Musa paradisiaca fruit using affinity chromatography. Binding interactions were examined using UV-Visible spectroscopy, circular dichroism (CD), differential scanning fluorimetry (DSF) and hemagglutination inhibition assay. Docking and molecular dynamics simulations were performed to analyze binding modes and complex stability. Additionally, the anticancer activity of Banlec and its drug-bound complexes was assessed against HL-60 cells using the MTT assay.

RESULTS

Banlec was purified from ripened Musa paradisiaca and characterized as a homodimeric protein (~30 kDa). UV-Visible spectroscopy confirmed spontaneous Banlec-drug interactions. CD analysis showed that Banlec retained its secondary structure upon binding with dasatinib and 5-FU, whereas pronounced conformational changes were observed with anastrozole. DSF analysis showed slight thermal stabilization with dasatinib and 5-FU, while anastrozole caused thermal destabilization. Hemagglutination inhibition assays indicated that the selected drugs did not mask the Banlec carbohydrate-binding domains and therefore its glycan-targeting potential is retained. Docking and MD simulations showed strongest binding with dasatinib, providing maximal stabilization, followed by 5-FU with moderate stabilization. Notably, among the evaluated complexes, Banlec-5-FU complex exhibited the most potent anticancer activity against HL-60 cells, compared to Banlec and 5-FU alone.

CONCLUSION

This study provides the first comprehensive insight into Banlec-anticancer drug interactions, identifying 5-FU as the most favorable binding partner. The findings highlight Banlec as a promising scaffold for development of glycan-targeted anticancer drug delivery systems and expand its therapeutic potential.