LAUSR

Understanding the transcytosis phenomenon through albumin binding receptor (glycoproteins) is an important step towards targeted drug delivery research. The transcytosis of bovine serum albumin (BSA) occurs through its uptake by binding to glycoprotein (gp60) present on the endothelial cell membrane. gp60 possess abundant glycans like N-acetylneuraminic acid (sialic acid, NANA), l-fucose (FUC), N-acetyl glucosamine (NAG), d-mannose (MAN) and d-galactose (GAL). Hence, the objective of the present study was to insight the binding between BSA-gold nanoparticles (GNPs) and BSA-silver nanoparticles (SNPs) conjugates with model glycans using several biophysical techniques. The fluorescence spectroscopy analysis established the strong affinity of BSA-NPs conjugates with glycan's as observed with the bimolecular quenching rate, the Stern-Volmer constant (Ksv), binding constant and binding site. The increase in hydrodynamic radii of conjugates exhibited strong association and zeta potential confirmed the significant stability of conjugates. Circular dichroism (CD) study showed that the substantial amount of secondary structure (α-helix) was retained in NPs bound BSA while interacting with glycans. Raman spectroscopy study of BSA-GNP and BSA-SNP with glycans depicted the intrusion in the spectral range of 400-1800 cm-1. The overall results showed that BSA-NPs conjugates can act as a virtuous system for targeted drug delivery in endothelial cells.