Insight into the binding of Nano-Berberine with alphalactalbumin: spectroscopic and molecular docking approaches

Alpha-Lactalbumin is the main whey protein in human milk. It has a key function in the synthesis of lactose from glucose and galactose in the mammary gland although this compound has also other beneficial effects on the infant health due to the high proportion of essential amino acids (tryptophan and cysteine)[1]. Berberine, a bioactive alkaloid isolated from several herbal substances, possesses multiple pharmacological effects, including antimicrobial, antidiabetic. Berberine has been reported to inhibit cell proliferation and to be cytotoxic towards cancer cells anticancer activities[2, 3]. In this study we reveal the Nano-Berberine effects upon interaction with Alpha-lactalbumin by using the biophysical methods and molecular docking.The secondary structure of alpha-lactalbumin has been changed upon interaction with Nanoberrberine that showed electrostatic forces induced. Stern-Volmer plots revealed the binding affinity of Nano-berberine to alpha-lactalbumin from the viewpoint of interaction behavior type.

Insight into the binding of Nano-Berberine with alphalactalbumin: spectroscopic and molecular docking approaches Keywords:

Nano-Berberine , Alpha-lactalbumin , Spectroscopy , Molecular docking