Interactions of cancer drugs with human serum albumin and membranes studying by NMR spectroscopy

The information on absorption, distribution, metabolism of drugs and also knowledge on the lifetime of drug in organs, are very important for the efficiency of a successful treatment. The most important factor for drugs injected to veins, is the binding affinity to human serum albumin. Human serum albumin (HSA) is the most abundant serum protein. The albumin has a binding capacity for many ligands, and it can bind drugs injected to vein. If the drugs bound to albumin are not dissociated, they may not reach to target tissue effectively. This knowledge implies that, the interaction between drug and albumin should be optimum for an effective treatment.In this study, for three different drugs (5-Fluorouracil (5-FU), Cytosine ß-D Arabinofuranoside (Ara-C), Cyclophosphamide-Monohydrate (CM)), drug-albumin interactions were investigated versus increasing drug and albumin concentration by 400 MHz NMR spectrometer. In this work, spectrums (peaks), chemical shifts and data related to relaxation times of peaks were used. The results obtained from these data gave us useful information about molecular dynamics of drug-albumin interactions. In this study, also, for three different drugs, drug-membrane interactions were investigated for two different membranes (normal and diabetic) versus increasing drug concentration and signal intensities and chemical shift values of membrane peaks were used.