Profenofos (PF) and captan (CT) are among the most utilized organophosphorus insecticides and phthalimide fungicides, respectively. To elucidate the physicochemical and influential toxicokinetic factors, the mechanistic interactions of serum albumin and either PF or CT were carried out in the current study using a series of spectroscopy and computational analyses. Both PF and CT could bind to bovine serum albumin (BSA), a representative serum protein, with moderate binding constants in a range of 10³–10⁴ M⁻¹. The bindings of PF and CT did not induce noticeable BSA’s structural changes. Both pesticides bound preferentially to the site I pocket of BSA, where the hydrophobic interaction was the main binding mode of PF, and the electrostatic interaction drove the binding of CT. As a result, PF and CT may not only induce direct toxicity by themselves, but also compete with therapeutic drugs and essential substances to sit in the Sudlow site I of serum albumin, which may interfere with the pharmacokinetics and equilibrium of drugs and other substances causing consequent adverse effects.

丙溴磷 (PF) 和克菌丹 (CT) 分别是最常用的有机磷杀虫剂和邻苯二甲酰亚胺杀菌剂。为了阐明物理化学和影响毒代动力学的因素，本研究使用一系列光谱学和计算分析来研究血清白蛋白与 PF 或 CT 的机械相互作用。 PF和CT均可与牛血清白蛋白（BSA）（一种代表性血清蛋白）结合，结合常数在10 ³ –10 ⁴ M ^-1范围内。 PF 和 CT 的结合不会引起 BSA 的结构发生明显变化。两种农药均优先与BSA的I位点结合，其中疏水相互作用是PF的主要结合方式，静电相互作用驱动CT的结合。因此，PF和CT不仅本身可能引起直接毒性，而且还与治疗药物和必需物质竞争坐在血清白蛋白的Sudlow位点I上​​，这可能干扰药物和其他物质的药代动力学和平衡，导致随之而来的不利影响。