Dipeptide carboxamide bearing nitrobenzene sulphonamides offers new prospect towards the inhibition of hemoglobin degradation in erythrocytes by Plasmodium falciparum; a malaria parasite and glycosyl phosphatidyl inositol (GPI) pathway which controls the release of variable surface glycoprotein (VSG) from Trypanosoma brucei. Structural design carried out produced series of dipeptide carboxamide bearing p-nitrobenzene sulphonamide compounds formed by coupling isoleucine (Ileu) or leucine (Leu) bearing amine with p-nitrobenzene sulphonamide bearing Ileu or Leu. Variation of coupling sequence between amidated amino acids and p-nitrobenzene sulphonamide bearing amino acid generates a library of 52 amidated Leu-Ileu dipeptide carboxamides bearing p-nitrobenzene sulphonamide compounds. Antimicrobial properties were evaluated using in-silico molecular docking. Protein residues E.coli (coded: 5MMN), plasmepsin (coded: 3QSI), trypanosome brucei dihydrofolate reductase pyrimethamine (coded: 3QFX) and prostaglandin synthese (coded: 1EQG) were generated from protein data base and was used to study biological activities of the compounds on bacterial, malarial, trypanosomiasis and analgesic parasites respectively. Ofloxacin, celecoxib, chloroquine and melarsoprol were used for docking studies as reference drugs for antibacterial, analgesic, antimalarial and antitrypanosomiasis respectively. Selected compounds from docking studies were examined using ADMET to ascertain their toxicity profile. Results of the antimicrobial properties reveal that some of the compounds showed better binding affinity on plasmepsin and trypanosome brucei parasites compared to standard drug used as reference in the docking studies, making them a potential drug candidates for malaria and trypanosomiasis treatment.