Park Jong-Ho, Kwon Eun-Young, Jung Hyo-Il, Kim Dae-Eun
Department of Mechanical Engineering, Yonsei University, Seoul, South Korea.
Biotechnol Lett. 2006 Apr;28(7):505-9. doi: 10.1007/s10529-006-0010-y.
The binding force between a liposome and the C2A domain of synaptotagmin I was determined by an atomic force microscopy (AFM). Liposomes were immobilized on the surface of the L1 sensor chip and the C2A domains, which recognize phosphatidylserine, were chemically conjugated onto a gold-coated cantilever tip. The average interaction force between the C2A domain and the liposome was 306 (+/-57) pN while the force between untreated cantilever and the liposome was 58 (+/-16) pN. This work helps understand the physicochemical interactions between proteins and lipid vesicles for the design of high affinity protein probes against the apoptotic cell surface.
通过原子力显微镜（AFM）测定了脂质体与突触结合蛋白I的C2A结构域之间的结合力。将脂质体固定在L1传感器芯片表面，而识别磷脂酰丝氨酸的C2A结构域化学偶联到镀金的悬臂尖端上。C2A结构域与脂质体之间的平均相互作用力为306（±57）皮牛，而未处理的悬臂与脂质体之间的力为58（±16）皮牛。这项工作有助于理解蛋白质与脂质囊泡之间的物理化学相互作用，以设计针对凋亡细胞表面的高亲和力蛋白质探针。
