Visfatin, otherwise known as Nicotinamide phosphoribosyltransferase (NAmPRTase or Nampt), is an adipocytokine that promotes B cell maturation and inhibits neutrophil apoptosis as well as promoting the condensation of nicotinamide. Visfatin plays an important role in promoting insulin resistance by binding to insulin receptor (IR) at a site distinct from insulin exerting a variety of insulin-mimetic effects, thereby playing a role in the development of obesity-associated insulin resistance and Type II diabetes. This research sought to understand binding interaction of pharmaceuticals to Visfatin. 11 crystal structures of the Visfatin were docked using IGEMDock to FDA, Alkaloids, Lactams, Lactones, Flavinoids, Sulfanilamide, Cyclic Imides, and NSAIDs drugs to determine structural correlation for the most effective binders. Structural similarities were determined with IGEMDock and vROCS and partition coefficient was determined using DRAGON program. This data found a cluster of potential inhibitors to Visfatin which are possible targets for Type II diabetes treatments. This research will be used in the engineering of improved Visfatin inhibitors.