Institute of Chemical Biology and Fundamental Medicine SB RAS, 630090 Novosibirsk, Russia.
Novosibirsk State University, 630090 Novosibirsk, Russia.
Molecules. 2020 Dec 29;26(1):108. doi: 10.3390/molecules26010108.
Pulsed Dipolar Spectroscopy (PDS) methods of Electron Paramagnetic Resonance (EPR) were used to detect and characterize reversible non-covalent dimers of Human Serum Albumin (HSA), the most abundant protein in human plasma. The spin labels, MTSL and OX063, were attached to Cys-34 and these chemical modifications of Cys-34 did affect the dimerization of HSA, indicating that other post-translational modifications can modulate dimer formation. At physiologically relevant concentrations, HSA does form weak, non-covalent dimers with a well-defined structure. Dimer formation is readily reversible into monomers. Dimerization is very relevant to the role of HSA in the transport, binding, and other physiological processes.
电子顺磁共振（EPR）的脉冲偶极子光谱（PDS）方法被用于检测和表征人血清白蛋白（HSA）的可逆非共价二聚体，HSA 是人血浆中最丰富的蛋白质。自旋标记物 MTSL 和 OX063 被连接到 Cys-34，这些 Cys-34 的化学修饰确实影响了 HSA 的二聚化，表明其他翻译后修饰可以调节二聚体的形成。在生理相关浓度下，HSA 确实与人血清白蛋白形成具有明确定义结构的弱非共价二聚体。二聚体形成很容易可逆为单体。二聚化与人血清白蛋白在运输、结合和其他生理过程中的作用非常相关。
