Abstract
Theophylline (THP), theobromine (THB) and caffeine (CAF) belong to the xanthine group of drugs and are principle component of tea or coffee with important pharmacological activities and clinical applications. The interaction between these drugs and serum albumin proteins obtained from bovine and human (BSA and HSA, respectively) in the presence and absence of silver as well as gold nanoparticles (Ag and AuNP, respectively) was investigated for the first time by using a series of biophysical techniques and molecular modelling calculations. Time resolved fluorescence measurements confirm that all the drugs quench the intrinsic tryptophan fluorescence of the proteins through a static mechanism irrespective of the absence or presence of NPs. However, the binding constant of the proteins towards the drugs changes considerably in presence of NPs. Addition of drugs decreases α-helicity of the proteins both in the absence and presence of NPs; however, no substantial change in protein secondary structure is perceived only with the NPs. The results show that the drug carrying capacity of the albumins can be significantly modulated with metal NPs towards desired pharmacokinetic and therapeutic applications without compromising the basic structure; and therefore, the function of the proteins.
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