Dipeptidyl Peptidase-IV (DPP-IV), an intracellular enzyme, plays a vital role in the management of diabetes mellitus via promoting secretion of insulin. Inhibitor of DPP-IV significantly improves the blood glucose and glycated hemoglobin A1c levels along with reducing adverse effects associated with current therapies. Extensive literature survey of DPP-IV inhibitors indicated that proline mimic pyrrolidine scaffold, demonstrated potent antidiabetic activity. Therefore, it was considered of interest to manually design and predict the mode and extent of binding of novel pyrrolidine derivatives using molecular docking studies by MVD software. The results of present studies revealed that the presence of bulky electropositive substituent at R1 while non bulky electronegative substituent at R2 position of pyrrolidine scaffold may be responsible for making expectant interactions with the key residue of DPP-IV enzyme active site. The information generated from the present work will be useful for the discovery of novel insulin promoter for the management of diabetes.