To investigate the interaction and adsorption of drug and carbon nanotube on human serum albumin, three anti-cancer drugs ([Pd(phen)(R-gly)]NO₃, R = methyl, propyl and amyl) with different hydrophobic tails and anticancer activities were selected. These drugs have better anti-tumor activity and less side effects than that known cis-platinum drug. Human serum albumin is also important for drug delivery and release and acts as carrier of internal biological molecules and external drugs that bind to many drugs in blood route and carry them. Drug binding to human serum albumin can change its helicity and this can affect on the drug release and distribution. Thus, study of this aspect can provide structural features determining the therapeutic efficiency of drug that has the least effect on human serum albumin helix structure. Interaction of three drugs with human serum albumin was investigated by molecular dynamics simulation and the best drug with the least denaturation effect was selected to compare its effect in the presence of nanotube. The structure of protein was again compared in the presence of drug and nanotube. The results revealed less denaturation effect of methyl on human serum albumin structure. The denaturation of protein also decreased more in the presence of nanotube. Carbon nanotube can be used as a cover for denaturation effect of drug and leads to better orientation and less random movement of drug around protein. It also reveals drug interaction with protein binding site facilitated in the presence of carbon nanotube.