Complementary characteristics of homologous p-octiphenyl β-barrels with ion channel and esterase activity Original Research Article

We report that decreasing β-sheet length in homologous multifunctional rigid-rod β-barrels with internal histidines increases ion channel stability by three orders of magnitude, reduces binding activity by four orders of magnitude, and reduces esterase activity up to 22-times. These results are further used to evaluate methods employed to characterize suprastructure and activity of synthetic multifunctional pores formed by p-octiphenyl β-barrels with emphasis on applicability of the Hille model to determine internal diameters and the Woodhull equation to locate internal active sites.