title: Chemical-induced pH-mediated molecular switch.
abstract: The transmembrane protein α-hemolysin pore has been used to develop ultrasensitive biosensors, study biomolecular folding and unfolding, investigate covalent and noncovalent bonding interactions, and probe enzyme kinetics. Here, we report that, by addition of ionic liquid tetrakis(hydroxymethyl)phosphonium chloride solution to the α-hemolysin pore, the α-hemolysin channel can be controlled open or closed by adjusting the pH of the solution. This approach can be employed to develop a novel molecular switch to regulate molecular transport and should find potential applications as a "smart" drug delivery method.
authors.affiliation: Department of Chemistry and Biochemistry, The University of Texas at Arlington, 700 Planetarium Place, Arlington, Texas 76019-0065, USA.
authors.forename: Dilani A
authors.initials: DA
authors.lastname: Jayawardhana
authors.forename: Mrinal K
authors.initials: MK
authors.lastname: Sengupta
authors.forename: D M Milan
authors.initials: DM
authors.lastname: Krishantha
authors.forename: Jyoti
authors.initials: J
authors.lastname: Gupta
authors.forename: Daniel W
authors.initials: DW
authors.lastname: Armstrong
authors.forename: Xiyun
authors.initials: X
authors.lastname: Guan
mesh_terms: D015374:Biosensing Techniques; D004573:Electrolytes / Q000737:chemistry; D006460:Hemolysin Proteins / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D052578:Ionic Liquids / Q000737:chemistry*; D007700:Kinetics; D017510:Protein Folding; D058767:Protein Unfolding; D047392:beta-Cyclodextrins / Q000737:chemistry
chemical_list: D004573:Electrolytes; D006460:Hemolysin Proteins; D052578:Ionic Liquids; D047392:beta-Cyclodextrins; C031215:betadex