Thermolysin-triggered short peptides self-assembly in confined space and application in cell culturing

Molecules self-assembly in confined space such as in cell to form microfilaments is a crucial process to achieve special functionality. Herein, short peptides with different sequences were taken as examples to explore their self-assembly behavior in AAO templates which offer different pore size and depth to mimic confined environment. Thermolysin, as a mild, selective and effective biological enzyme, is applied here to trigger the self-assembly of short peptides in the pores of AAO template. Experimental results indicate that the morphology, structure and orientation of short peptide fibers in the pores are significantly affected by pore size of AAO templates. Moreover, the formed short peptide fibers in pores show obvious influence on the cell morphology and spreading. The method proposed here gives a feasible avenue to reveal the effect of confined environment on self-assembly behavior of short peptide.