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A capillary electrophoresis strategy to sensitively detect dynamic properties of coiled coil polypeptides
Author(s) -
Yang Jie,
Zhao SunDuo,
Zhao DongHui,
Huang Yan,
Liu XiaoXia,
Hu Wei,
Liu Bo
Publication year - 2020
Publication title -
journal of separation science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.72
H-Index - 102
eISSN - 1615-9314
pISSN - 1615-9306
DOI - 10.1002/jssc.202000137
Subject(s) - macromolecule , chemistry , coiled coil , electromagnetic coil , förster resonance energy transfer , energy exchange , capillary electrophoresis , capillary action , analytical chemistry (journal) , random coil , chromatography , materials science , crystallography , biochemistry , optics , fluorescence , circular dichroism , physics , atmospheric sciences , composite material , geology , electrical engineering , engineering
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 PC 10 and PC 10 P were designed and biosynthesized. PC 10 and PC 10 P could form nanogels when the concentration of polypeptides was less than 2% (m/v). The dynamic behaviors of PC 10 and PC 10 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.
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