Spectroscopic and molecular modelling studies on glycation modified bovine serum albumin with cyanidin-3-O-glucoside.

摘要: Abstract In this study, we report the glycation mediated effect of bovine serum albumin (BSA) on molecular interaction mechanism cyanidin-3-O-glucoside (C3G) by modelling, Uv–visible spectroscopy, transmission electron microscopy (TEM), fluorescence and circular dichroism spectroscopy studies. The structures advanced end-products (AGEs) modified BSA were modelled, energy minimized analyzed for binding affinity docking studies using Autodock Vina. Glycation experiments are carried out glucose methylglyoxal to validate modelling results with C3G. characterized reduction in pocket volume, surface, depth, hydrophobicity, hydrogen bond donors/acceptors. Arg-194, Arg-196, Arg-198, Arg-217, Arg-409, Lys-114, Lys-116, Lys-204, Lys 221, Lys-439 found be crucial context BSA. TEM images represented formation unique globular aggregates event glycation. spectroscopic showed new chromophores between 300 400 nm Fluorescence quenching was observed a differential manner presence C3G Circular suggested loss helical structure β-sheeted upon glycation, but subsequent has resulted increase towards structure. Our findings that drug been certainly impaired due AGE modification. Arg-p modification more austere impact would affect properties. We conclude had modulation properties glycated which can help protect stability bioavailability structural changes.