Possible denaturation or tertiary structural changes of the protein human serum albumin (HSA) upon adsorption of uremic toxin is investigated using small-angle neutron scattering (SANS). Calorimetric data in previous studies give proof of the binding between HSA and two classes of uremic toxins: i) small molecular weight and ii) middle molecular weight molecules. A representative polyelectrolyte of negative net charge is used as a model middle molecule and two molecules phenylacetic acid (PhAA) and indoxyl sulfate (IDS) represent the small molecular weight toxins. The present study find no proof of destabilization of the protein structure upon toxin uptake. Analyzing the structure factor of scattering intensities from high concentrated protein samples complexed with PhAA and IDS show that interaction between native and complexed HSA is also not altered. However, a small effect of the net charge of HSA is found in the case of urea modified proteins.

使用小角度中子散射（SANS）研究了尿毒症毒素吸附后人血清白蛋白（HSA）蛋白质可能的变性或三级结构变化。先前研究中的量热数据提供了HSA与两类尿毒症毒素之间结合的证据：i）小分子量和ii）中分子量分子。负净电荷的代表性聚电解质用作模型中间分子，苯乙酸（PhAA）和硫酸吲哚酚硫酸盐（IDS）这两个分子代表小分子量毒素。本研究没有发现毒素吸收后蛋白质结构不稳定的证据。分析与PhAA和IDS复合的高浓度蛋白质样品的散射强度的结构因子表明，天然和复合HSA之间的相互作用也没有改变。但是，对于尿素修饰的蛋白质，HSA净电荷的影响很小。