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Complementary Characteristics of Homologous p-octiphenyl β-Barrels with Ion Channel and Esterase Activity

Published inBioorganic & medicinal chemistry, vol. 11, no. 7, p. 1363-1369
Publication date2003
Abstract

We report that decreasing ß-sheet length in homologous multifunctional rigid-rod ß-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 ß-barrels with emphasis on applicability of the Hille model to determine internal diameters and the Woodhull equation to locate internal active sites.

Citation (ISO format)
SOM, Abhigyan, SAKAI, Naomi, MATILE, Stefan. Complementary Characteristics of Homologous p-octiphenyl β-Barrels with Ion Channel and Esterase Activity. In: Bioorganic & medicinal chemistry, 2003, vol. 11, n° 7, p. 1363–1369. doi: 10.1016/S0968-0896(02)00620-X
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