Zhang Yuai, Cao Yiqing, Li Yan, Zhang Xuemei
Department of Pharmacology, School of Pharmacy, Fudan University, Shanghai 201203, China.
NanChang Bozekang Pharmaceutical Technology Co., Ltd., Nanchang 330000, China.
Molecules. 2022 Feb 24;27(5):1526. doi: 10.3390/molecules27051526.
Sulfonamides are widely used antibiotics in agricultural production. However, the potential threat of these drugs to human health has increased global concern. Human serum albumin (HSA) is the main reservoir and transporter of exogenous small molecules in humans. In this study, the interaction between sulfadimethoxine (SMT) and human serum albumin (HSA) was studied using spectroscopy and computer simulation. Our results showed that the hydrogen bonding and van der Waals forces drove SMT to enter the binding site I of HSA spontaneously and resulted in the fluorescence quenching of HSA. The stability of the HSA-SMT complex decreased with an increase in temperature. The binding of SMT to HSA induced alterations in the secondary structure of HSA, where the content of α-helix decreased from 61.0% of the free state to 59.0% of the compound state. The π-π, π-σ, and π-alkyl interactions between HSA and SMT were found to play important roles in maintaining the stability of the complex.
磺胺类药物是农业生产中广泛使用的抗生素。然而，这些药物对人类健康的潜在威胁已引起全球关注。人血清白蛋白（HSA）是人体内外源小分子的主要储存库和转运体。在本研究中，采用光谱学和计算机模拟方法研究了磺胺二甲氧嘧啶（SMT）与人血清白蛋白（HSA）之间的相互作用。我们的结果表明，氢键和范德华力驱动SMT自发进入HSA的结合位点I，并导致HSA的荧光猝灭。HSA-SMT复合物的稳定性随温度升高而降低。SMT与HSA的结合诱导了HSA二级结构的改变，其中α-螺旋含量从游离状态的61.0%降至复合状态的59.0%。发现HSA与SMT之间的π-π、π-σ和π-烷基相互作用在维持复合物的稳定性中起重要作用。
