Abstract
Enteromorpha prolifera (E. prolifera), a tonic food in East Asian countries, is frequently studied for their pharmaceutical and healthcare applications. However, limited research has focused on antitumor peptides derived from this edible seaweed. In this study, we aimed to investigate the anticancer properties of peptides isolated from the hydrolysate of E. prolifera generated by a plethora of proteases including trypsin, papain, bromelain, and alkaline protease. The results showed that the hydrolysate produced by papain digestion exhibited remarkably stronger anticancer activity and was subjected to further purification by ultrafiltration and sequential chromatography. One heptapeptide, designated HTDT-6-2-3-2, showed significant antiproliferation activity towards several human cancer cell lines. The IC50 values for NCI-H460, HepG2, and A549 were 0.3686 ± 0.0935 mg/mL, 1.2564 ± 0.0548 mg/mL, and 0.9867 ± 0.0857 mg/mL, respectively. Moreover, results from flow cytometry confirmed that cell apoptosis was induced by HTDT-6-2-3-2 in a dose-dependent manner. The amino acid sequence for this heptapeptide, GPLGAGP, was characterized by Edman degradation and further verified by Liquid Chromatography-Tandem Mass Spectrometry. In silico analysis results suggested that XIAP could be a potential target for HTDT-6-2-3-2. Molecular docking simulation showed that HTDT-6-2-3-2 could occupy a shallow pocket in the BIR3 domain of XIAP, which is involved in the inhibitory effect of caspase-9 activation. In conclusion, this E. prolifera derived peptide exhibited strong anticancer properties, which could be explored for pharmaceutical applications.
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