Peptidomimetics is a novel drug designing strategy in which an Insilico inhibitor is designed by mimicking the framework of a short peptide. Novel drug design strategies shall only pave way for developing unique and safer anti-HIV drugs. In the present study, we propose a Peptidomimetics based gp120 attachment inhibitor. In human biological system, HIV-1 interacts with CD4 receptor of the host via its surface glycoprotein gp120 establishing initial attachment. This protein-protein interaction interface forms the base to derive an inhibitor mimicking backbone of the receptor. The mimicked inhibitor derived in this study is based on the insilico interactions of soluble CD4 (SCD4) (precursor of CD4) with gp120. The molecular interactions of SCD4 with gp120 were identified by MEDock software. Furthermore, the interacting interface was analyzed manually for topology, and the backbone of the ligand molecule was sketched based on it with chemsketch. Moreover, the sketched ligand was optimized and was docked with gp120 using Argus lab. Docking results show six hydrogen bonds formation between the ligand and binding interface of gp120. The ligand was also found to be fit with good druggable character, as per Lipinski's rule of five. Hence, this work addresses the drug likeness of the peptidomimetic ligand proposed.