Human immunodeficiency virus-1 (HIV-1) infection continues to be a major medical threat to humans. In anti-HIV therapies, HIV-1 protease (HIVP) is still one of the most important targets. It has been reported that sugar hybrids have the ability to interact with the HIVP.

The study of the interactions with the active site of HIVP of hybrids which contain two sugar units across a malonate spacer (type I) was examined through Molecular Docking simulations. Due to the ability of steroid to increases the biocompatibility of the hybrids, was also performed the docking studies of carbohydrate-steroid conjugates (type II). In order to analyze the binding interactions between the ligands and HIVP was employed the Autodock Vina program. All the studied derivatives presented binding energies of -10 to -12 kcal/mol. However, the ligand type II occluded the active site of the protease with a major affinity than ligand type. The results suggested that type II hybrids could be used as potential inhibitors of HIVP.

Hence, in this work we report for first time the synthesis of two steroid-monosaccharide conjugates through several steps. The first one was the preparation of the required starting malonates to obtain a new steroidal acid. On the other hand, the monosaccharides are selectively protected using standard methodologies for further condensation with the steroidal acid to obtain the monosaccharide-steroid conjugates. The synthetized compounds were characterized employing modern spectroscopic techniques by NMR and Mass Spectrometry has allowed the chemical structures of the new compounds to be unambiguously determined.