Complementary characteristics of homologous p-octiphenyl beta-barrels with ion channel and esterase activity.
We report that decreasing beta-sheet length in homologous multifunctional rigid-rod beta-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 beta-barrels with emphasis on applicability of the Hille model to determine internal diameters and the Woodhull equation to locate internal active sites.
Som
Abhigyan
A
Department of Organic Chemistry, University of Geneva, CH-1211 Geneva 4, Switzerland.
Sakai
Naomi
N
Matile
Stefan
S
D000465:Algorithms; D004305:Dose-Response Relationship, Drug; D004791:Enzyme Inhibitors / Q000138:chemical synthesis* / Q000494:pharmacology*; D004950:Esterases / Q000037:antagonists & inhibitors*; D015640:Ion Channel Gating / Q000187:drug effects; D007473:Ion Channels / Q000187:drug effects*; D007700:Kinetics; D008051:Lipid Bilayers; D008968:Molecular Conformation; D009842:Oligopeptides / Q000138:chemical synthesis / Q000494:pharmacology; D017433:Protein Structure, Secondary
D004791:Enzyme Inhibitors; D007473:Ion Channels; D008051:Lipid Bilayers; D009842:Oligopeptides; D004950:Esterases