Visc ometery and Spectral Investigation on Interaction of Cu(II)Salen Co mplex and Bovine Serum Alb umin: A Thermod ynamic ap proach

In recent years, me tal complexes with sa len ligands derived from the co ndensation of salicylal dhyde with a diamine, h ave been widely studied [۱]. Many compound s expose their antitumor activity through binding to DNA and can cause DNA damage in ca ncer cells b y blocking the division of cancer cells and resulting in cell death [ ۲]. Serum albumin is t he most abu ndant protein in the circulatory system of a wide variety of organisms and plays an important role in the transport and depositio n of many drugs. Thus, an understanding of t he features of drug interactions with albumin can provide insights into chemo ther apy and dru g design. B ovine seru m albumin (BSA) is usu ally emplo yed as a model protein because of its low cost and availa bility and because it is structurally homolo gous with human serum albumin[۳]. In this w ork the interaction of Cu(ǿǿ)Salen with BSA w as studied using UV/Vis spectrosc opic method.

کلیدواژه ها:

Metallosa len ، Cu(II)S alen ، Bovine serum alb umin(BSA) ، Binding iso therm.