Acrylamide is a neurotoxic and carcinogenic organic compound that is able to bind to several biomolecules and form adducts, through nucleophilic addition and in vivo by the Maillard Reaction, interfering with the biological functions of these molecules. Hemoglobin is one of the most abundant intracellular blood proteins, and thus it is of high interest to understand whether the binding of acrylamide can alter its properties. The interaction of acrylamide with hemoglobin was assessed in a 20:1 ratio, and after a 72 h-incubation period, a decrease of ca. 50% in the absorbance of the hemoglobin's Soret band was observed at 37 °C. This together with the analysis of circular dichroism spectra indicate that acrylamide binds in close proximity to the heme group. These perturbations were confirmed to not correspond to the loss of the heme group and were mostly reverted after passing the protein through a size-exclusion chromatographic matrix, suggesting a dominant non-covalent interaction for the observed effect. The thermodynamic parameters of unfolding in the absence and presence of acrylamide, suggest an interaction based on H-bonds and van der Waals forces that slightly stabilizes hemoglobin. The oxygen binding capacity of hemoglobin does not seem to be hindered, as no differences in the Q bands were observed in the adduct.

丙烯酰胺是一种具有神经毒性和致癌性的有机化合物，能够通过亲核加成和体内结合到多种生物分子上并形成加合物通过美拉德反应，干扰了这些分子的生物学功能。血红蛋白是最丰富的细胞内血液蛋白之一，因此，了解丙烯酰胺的结合是否可以改变其特性具有很高的兴趣。丙烯酰胺与血红蛋白的相互作用以20：1的比例进行评估，并且在72小时的孵育时间后，大约减少了。在37°C下观察到血红蛋白Soret带的吸收率为50％。这与对圆二色性光谱的分析一起表明，丙烯酰胺与血红素基团紧密结合。这些扰动被证实与血红素基团的丢失不相符，并且在使蛋白质通过尺寸排阻色谱矩阵后大部分恢复，表明观察到的作用是主要的非共价相互作用。在不存在和存在丙烯酰胺的情况下，展开的热力学参数表明，基于氢键和范德华力的相互作用会稍微稳定血红蛋白。似乎并未阻碍血红蛋白的氧结合能力，因为在加合物中未观察到Q带的差异。