三价离子存在下浓缩牛血清白蛋白溶液的桥联吸引力：小角中子散射研究。
Bridging attraction of condensed bovine serum albumin solution in the presence of trivalent ions: A SANS study.
机构信息
NHC Key Laboratory of Nuclear Technology Medical Transformation, Mianyang Central Hospital, School of Medicine, University of Electronic Science and Technology of China, Mianyang 621000, China.
Key Laboratory of Neutron Physics and Institute of Nuclear Physics and Chemistry, China Academy of Engineering Physics, 621999 Mianyang, China.
出版信息
Biochim Biophys Acta Gen Subj. 2023 Dec;1867(12):130487. doi: 10.1016/j.bbagen.2023.130487. Epub 2023 Oct 6.
The bridging attraction of condensed bovine serum albumin (BSA) solution (DO) in the presence of yttrium chloride (YCl) was studied by small angle neutron scattering (SANS). With increasing the concentration of YCl (c) from 3 to 15 mM and from 15 to 100 mM, the intensity in low-q region increases and then decreases. Combining the tri-axial ellipsoid (TaE) geometry and the multi-component sticky hard sphere (SHS) potential, a SHS-TaE model was established to quantitatively determine the size and distribution of particles. In this way, the structural mechanism of the aggregation-redissolution process in protein solution was demonstrated and discussed. As c increases from 3 to 100 mM, the SHS radius r decreases from ca. 2.97 to 2.50 nm, suggesting that the relatively well dispersed BSAs may form aggregates with various polydispersities. The axis a increases from 1.88 to 2.30 nm, while b and c decrease from 3.53 to 3.23 nm and from 4.12 to 3.55 nm, respectively. (R decreases from ca. 2.57 to 2.38 nm). Moreover, the scattering length density (SLD) of BSA decreases from 3.67 to 1.56 × 10 Å. All these results consistently indicate a strengthened attraction and the BSA molecules might shrink and tune out to be more like of oblate ellipsoid with increasing the amount of YCl.
在氯化钇（YCl）存在下，通过小角中子散射（SANS）研究了凝聚态牛血清白蛋白（BSA）溶液的桥接吸引力。随着 YCl 浓度（c）从 3 mM 增加到 15 mM，再增加到 100 mM，低 q 区域的强度增加，然后降低。结合三轴椭球（TaE）几何形状和多组分粘性硬球（SHS）势，建立了 SHS-TaE 模型，以定量确定颗粒的大小和分布。通过这种方式，证明并讨论了蛋白质溶液中聚集-再溶解过程的结构机制。随着 c 从 3 mM 增加到 100 mM，SHS 半径 r 从约 2.97 nm 减小到 2.50 nm，表明相对分散良好的 BSA 可能形成具有各种多分散性的聚集体。轴 a 从 1.88 nm 增加到 2.30 nm，而 b 和 c 分别从 3.53 nm 减小到 3.23 nm，从 4.12 nm 减小到 3.55 nm（R 从约 2.57 nm 减小到 2.38 nm）。此外，BSA 的散射长度密度（SLD）从 3.67 Å 减小到 1.56×10 Å。所有这些结果都一致表明吸引力增强，随着 YCl 量的增加，BSA 分子可能收缩并调整为更扁的椭球体。
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