Abstract

Glycoproteins have emerged as promising agents in drug delivery due to their potential for targeted delivery. This study developed and evaluated complexes of Pentagamavunon-1 (PGV-1) with glycated bovine serum albumin to enhance cytotoxic effects against cancer cells. Bovine serum albumin nanoparticles (BSA NPs) and glycated BSA nanoparticles [BSA+Lactose (Lac) NPs] were synthesized and complexed with PGV-1. These complexes were characterized by particle size analysis, scanning electron microscopy, transmission electron microscopy, and Fourier transform infrared spectroscopy to confirm their successful synthesis and morphological properties. Cytotoxicity was assessed in HepG2, T47D, and Vero cell lines using MTT assays, while cellular senescence was evaluated by senescence-associated β-galactosidase staining. The results indicated that PGV-1+BSA+Lac NPs significantly increased cytotoxicity in HepG2 and T47D cancer cells compared to free PGV-1, while showing lower toxicity toward non-cancerous Vero cells and demonstrating enhanced selectivity. Furthermore, senescence analysis revealed reduced β-galactosidase activity in Vero cells treated with PGV-1+BSA+Lac NPs relative to free PGV-1, supporting the targeted action of these nanoparticles. In conclusion, PGV-1+BSA+Lac NPs not only improve the delivery efficiency and selectivity of PGV-1 but also present a promising strategy for cancer-specific drug delivery. This research advances the development of glycoprotein-based delivery systems, offering a potential platform for targeted cancer therapies.

Key words: Pentagamavunon-1, Complexes, Glycated BSA, characterization, cytotoxic