Department of Physics and Astronomy, University of Texas at San Antonio, San Antonio, TX, USA.
Protein J. 2013 Aug;32(6):493-504. doi: 10.1007/s10930-013-9508-z.
Human serum albumin (HSA) has been used as a model for the binding of a number of different ligands, including polyaromatic hydrocarbons, to proteins. In this case we have investigated the interaction of HSA with a novel set of perylene derivatives. Di-substituted perylene analogues have been synthesized as potentially useful organic photovoltaic materials. Their photophysical properties may make them viable for fuel cell applications too. However, these molecules are poorly soluble especially in aqueous solvents. Binding to water-soluble proteins may provide a way to solubilize them. At the same time one can study whether the photophysical processes initiated by the irradiation of a perylene ligand can cause conformational changes to the host protein. With the present study we demonstrated that of the three perylene derivatives investigated only one, the dimethoxy analogue, has a significant affinity for HSA at a binding site near the bottom of the central cleft (in proximity of the Trp214 residue). The small affinity prevents any significant photoinduced changes to occur in the protein.
人血清白蛋白 (HSA) 已被用作结合许多不同配体（包括多环芳烃）的模型，以与蛋白质结合。在这种情况下，我们研究了 HSA 与一组新型苝衍生物的相互作用。二取代的苝类似物已被合成作为潜在有用的有机光伏材料。它们的光物理性质也可能使它们适用于燃料电池应用。然而，这些分子的溶解度很差，特别是在水性溶剂中。与水溶性蛋白质结合可能是一种增溶的方法。同时，人们可以研究由苝配体的辐照引发的光物理过程是否会导致宿主蛋白质发生构象变化。通过本研究，我们证明在所研究的三种苝衍生物中，只有一种，即二甲氧基类似物，在靠近中央裂缝底部（靠近色氨酸 214 残基）的结合位点与 HSA 具有显著的亲和力。这种小的亲和力阻止了蛋白质发生任何显著的光诱导变化。
