Cryptocarya pulchrinervia is an Indonesian indigenous plant that grows in Sumatra, Kalimantan and Papua. One of the new compounds extracted from this plant was cryptobrachytone C, which was known to be cytotoxic against cancer cells of Murine leukemia P388 with IC50 10.52 μM. In this study, the cytotoxicity and anticancer properties of cryptobrachytone C on proliferation, apoptosis, migration and clone formation of MCF-7 and T47D breast cancer cell lines were examined, which had not previously been done before. The cytotoxicity of the compound was measured using an MTT (3- (4,5-dimethylthiazol-2- yl) -2,5-di-phenyl-tetrazolium bromide) assay. The cell proliferation was measured using a BrdU assay, and the cell apoptosis was measured using annexin-V FITC, while the cell migration was measured using a transwell filter. The cytotoxic test result demonstrated that cryptobrachytone C was cytotoxic against MCF-7 cells with IC50 12.94 ± 0.32 μM but not against T47D cells with IC50 65.33 ± 2.33 μM nor against normal MRC-5 cells with IC50 122.57 ± 19.84 μM. The cell proliferation assay showed that cryptobrachytone C at IC50 concentration had antiproliferative properties against MCF-7 cancer cell lines (p < 0.05) but did not significantly reduce T47D cell proliferation (p < 0.07). Although the results of the cell apoptosis test showed that cryptobrachytone C could induce the apoptosis of the MCF-7 and T47D cells, it was insignificant (p > 0.05). The cell migration test showed that cryptobrachytone at IC50 concentrations could inhibit the migration of the MCF-7 and T47D cells. The clonogenic test showed that cryptobrachytone C at IC50 concentration can induce the inhibition of the formation of MCF-7 and T47D cell colonies. The cryptobrachytone C anti-cancer character was more signi icant on the MCF-7 cell line compared to the T47D. This study showed that cryptobrachytone C was cytotoxic and had potential as an anti-cancer compound against MCF-7 and T47D breast cancer cell lines.
Banana Lectin (BanLec) is a mannose-binding jacalin-related lectin that has attracted considerable scientific interest due to its affinity toward high-mannose-type N-glycans and its immunomodulatory and antiviral properties. It also has the potential to suppress cancer cell proliferation and stimulate macrophage activity. In this study, evolutionary relationships among BanLec sequences across the Musa genus were also examined, while the primary focus was the identification and characterization of BanLec-encoding genes from Musa acuminata subsp. malaccensis (Malaysian Dwarf Banana) and Musa balbisiana (Banana Klutuk Wulung), with emphasis on their molecular properties and potential interactions with a hypermannosylated N-glycan structure (Man8GlcNAc2) reported to be abundant in breast cancer. Seven and four high-confidence BanLec protein sequences were identified from M. acuminata subsp. malaccensis and M. balbisiana genomes, respectively, which all share conserved structural domains characteristic of BanLec with variable exon-intron organizations. Gene locations, duplications, and synteny analyses revealed lineage-specific diversification of lectin genes within each species and between the two Musa genomes. The identified BanLec proteins were modelled and then evaluated by molecular docking and molecular dynamics simulations using a hypermannosylated N-glycan structure. The computational binding analyses demonstrate that BanLec variants from different Musa genomes exhibit distinct energetic and structural preferences toward the hypermannosylated N-glycan structure. Among the tested complexes, Ma09_t10450 (M. acuminata subsp. malaccensis) showed the most stable interaction, followed by Mba09_g09930 (M. balbisiana), each demonstrating strongly favourable binding free energies (ΔG ≤ -22.43 ± 3.01 kcal mol⁻¹ and ΔG ≤ -17.87 ± 10.81 kcal mol⁻¹ respectively) and therefore considered suitable candidates for lectin binding assays conducted at neutral pH, 300 K, and physiological ionic strength. These findings strengthen BanLec's potential as a promising candidate for lectin-based biomarker development and glycan-targeted therapeutic applications.