Du Qiqige, Li Wanrong, Yuan Ming, Gong Pei, Zhang Yi, Zhang Feng
Agricultural Nanocenter, School of Life Sciences, Inner Mongolia Agricultural University, Hohhot, China.
Key Laboratory of Interfacial Physics and Technology, Shanghai Institute of Applied Physics, Chinese Academy of Sciences, Shanghai, China.
Luminescence. 2017 Jun;32(4):618-624. doi: 10.1002/bio.3229. Epub 2016 Oct 12.
Physisorptions occurs everywhere and constantly in living organisms and between nanomaterials and biomolecules. In this study, one of the most important proteins, G-actin, was selected to investigate its bio-nano physisorption with a model nanoparticle coated with a amphiphilic polymer. Using a photoluminescence quenching method, both the binding constant and the Hill constant were determined as 1.79 × 10 M and 0.84, respectively. Thermodynamic calculations proved that such a physisorption was a spontaneous procedure. The physisorption-mediated protein-nanoparticle conjugates were robust enough to resist gel electrophoresis, and protein conformation was kept intact, as revealed using circular dichroism. This conjugate might be a promising candidate for nanofabrication or could play a significant role in actin-related bioactivities.
物理吸附在生物体以及纳米材料与生物分子之间无处不在且持续发生。在本研究中，选取了最重要的蛋白质之一G-肌动蛋白，以研究其与包覆两亲聚合物的模型纳米颗粒的生物纳米物理吸附。采用光致发光猝灭法，测得结合常数和希尔常数分别为1.79×10 M和0.84。热力学计算证明这种物理吸附是一个自发过程。如使用圆二色性所揭示的，物理吸附介导的蛋白质-纳米颗粒缀合物足够稳定，能够抵抗凝胶电泳，并且蛋白质构象保持完整。这种缀合物可能是纳米制造的一个有前途的候选物，或者可能在肌动蛋白相关的生物活性中发挥重要作用。
