F11-R receptor was characterized as an adhesion protein, called also aka JAM-A (or JAM-1), which under normal physiological conditions is expressed constitutively on the surface of the platelets and localized within tight junctions of endothelial cells (EC). The utilization of specific F11R/JAM-A peptide antagonists and recombinant proteins supported the role of F11R/JAM-A in the process of platelets adhesion to inflamed endothelial cells and identified plaque formation leading to inflammatory thrombosis and atherosclerosis where the platelets have a critical influence in the progression and development of the cardiovascular disease. Thus, the development of new drugs antagonizing the F11R/JAM-A function could evolve as an effective strategy for the treatment of atherosclerosis, heart attacks and stroke. We present one of the first trials toward development of peptide-based inhibitors of F11R/JAM-A function. Among many trials, the peptide D-Lys-Ser-Val-Ser-D-Arg-Glu-Asp-Thr-Gly-Thr-Tyr-Thr-Cys-CONH2 proved to be a potent inhibitor of human platelets aggregation in vitro. Further molecular docking experiments showed that this peptide makes favorable hydrophobic and electrostatic interactions within the proposed binding site of JAM-1 (X-Ray structure 1nbq.pdb was used as template).