Actin filament senses mechanical forces and it is transduced into biochemical signals during many cellular processes. In the disassembling process of actin filaments, cofilin plays a central role as the actin filament depolymerization. In this study, we evaluated a quantitative analysis of the actin filament-cofilin interaction change dependent upon the actin filament curvature decrease using atomic force microscopy (AFM) and a fabricated wave-like substrate. A wave-like substrate was fabricated by a maskless photo-lithography of a spin coated film on a glass substrate, and graphene oxide sheet was used for the decreasing of non-specific interaction between protein and the substrate. By single-molecule force spectroscopy, we determined rupture force of actin filament-cofilin binding on the wave-like substrate and a flat substrate. The rupture force of actin filament-cofilin binding at the curvature of -1.35 μm-1 showed a value approximately 4 times higher than the rupture force at the curvature of -0.15 μm-1. The present study will provide the possibility and quantitative evidence that mechanical stress on cytoskeletal filaments can modulate how they interact with their binding proteins.
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