Darżynkiewicz Zbigniew M, Sławski Jakub, Rydzy Małgorzata, Grzyb Joanna
Łukasiewicz Research Network - PORT Polish Center for Technology Development, Stabłowicka 147, 54-066 Wrocław, Poland.
Department of Biophysics, Faculty of Biotechnology, University of Wrocław, F. Joliot-Curie 14a, 50-383 Wrocław, Poland.
ACS Omega. 2025 Jul 3;10(27):29628-29636. doi: 10.1021/acsomega.5c03139. eCollection 2025 Jul 15.
Protein binding to the colloidal quantum dot (QD) is necessary for the construction of nanobiohybrids. The calculation of stoichiometry may not be simple; QD is a sphere with a uniform surface, and the QD-protein junction may influence protein conformation and shape. Protein shape allows for different packing on the QD surface. Herein, we characterized binding between two types of QDs, differing by their radii, and three versions of a cytochrome c protein, native one, and with 6xHisTag on N- or C-terminus. The average stoichiometry was 2.44/8-9 protein molecules per nanoparticle, depending on QD. The binding of HisTag-proteins to QD was enthalpy-driven, with negative entropy. We verified the binding constants in different methods, allowing the exposition of the different surfaces of cytochrome c for binding.
蛋白质与胶体量子点（QD）的结合是构建纳米生物杂交体所必需的。化学计量的计算可能并不简单；量子点是具有均匀表面的球体，量子点与蛋白质的连接可能会影响蛋白质的构象和形状。蛋白质形状允许在量子点表面有不同的堆积方式。在此，我们表征了两种半径不同的量子点与细胞色素c蛋白的三种变体（天然型以及在N端或C端带有6xHis标签的变体）之间的结合。平均化学计量为每个纳米颗粒2.44/8 - 9个蛋白质分子，这取决于量子点。His标签蛋白与量子点的结合是由焓驱动的，熵为负。我们用不同方法验证了结合常数，从而使细胞色素c的不同表面得以暴露用于结合。
