Acrylamide (AA) is a carcinogenic compound found in food ingredients. The hemoglobin (Hb)-based AA biosensor was then developed because of biocompatibility and the capacity of Hb to join with other molecules. Hb was developed because it is an active bioreceptor protein that can bind to AA to form Hb-AA adduct. In this study, a computational study was carried out to perform molecular docking simulations for AA and other compounds to the N-terminal valine site of Hb, while both molecular interactions between the complexes and the obtained, ΔGbinding value were analyzed in this study. The results obtained in this study showed the ΔGbinding value of all interferent compounds were lower than that of AA with sodium acetate as the exception. The ΔGbinding at the residual Hb branch of valine-a, which interacted to ascorbic acid was -5.9269 kcal/mol, while to caffeine was -5.66429 kcal/mol, to glucose was -6.0497 kcal/mol, to sodium acetate was -3.6654 kcal/mol mole, and to melamine was -4.8279 kcal/mol. In the valine-β residues, ΔGbinding of ascorbic acid was -5.6727 kcal/mol, caffeine was -5.9915 kcal/mol, glucose was -6.022 kcal/mol, sodium acetate was -3.7198 kcal/mol, and melamine was -4,8021 kcal/mol. Therefore, it can be concluded that all these compounds compete with AA to bind to Hb, while AA is easier to use with Hb in the valine-a residue.