A capillary electrophoresis strategy to sensitively detect dynamic properties of coiled coil polypeptides.

The self-assembly behavior of polypeptides plays an essential role to form biological and functional macromolecules, which have attracted a lot of attention due to their excellent characters. Understanding the polypeptide self-assembly systems and dynamic behaviors is fundamental to improve the potential of biomedical applications. In this work, coiled coil polypeptides PC10 and PC10 P were designed and biosynthesized. PC10 and PC10 P could form nanogels when the concentration of polypeptides was less than 2% (m/v). The dynamic behaviors of PC10 and PC10 P were measured by Förster resonance energy transfer method based on a capillary electrophoresis system. The Förster resonance energy transfer efficiency of this system was 60.4%, and the distance of self-assembled domains in the polypeptides was calculated as 6.14 nm, demonstrating that the exchange behavior occurred between two different polypeptides containing the same coiled coil region.