title: Binding of organic anions by synthetic supramolecular metallopores with internal Mg2+-aspartate complexes.
abstract: We report that cation-selective transmembrane pores formed by synthetic p-octiphenyl beta barrels with internal aspartate residues can be transformed into anion-permeable metallopores with internal Mg(2+)-aspartate complexes. These metallopores are shown to be useful for fluorimetric sensing of a broad variety of organic anions of biological relevance such as phytate, heparin, thiamine phosphates, and adenosine triphosphate. The negligible flippase activity measurable for Mg(2+)-free pores indicates that transmembrane p-octiphenyl beta barrels do not disturb the lipid bilayer suprastructure, in other words, they form barrel-stave rather than toroidal pores.
authors.affiliation: Department of Organic Chemistry University of Geneva 1211 Geneva 4, Switzerland.
authors.forename: Gopal
authors.initials: G
authors.lastname: Das
authors.forename: Hisanari
authors.initials: H
authors.lastname: Onouchi
authors.forename: Eiji
authors.initials: E
authors.lastname: Yashima
authors.forename: Naomi
authors.initials: N
authors.lastname: Sakai
authors.forename: Stefan
authors.initials: S
authors.lastname: Matile
mesh_terms: D000838:Anions / Q000737:chemistry; D001224:Aspartic Acid / Q000737:chemistry*; D002352:Carrier Proteins; D007476:Ionophores / Q000737:chemistry*; D008051:Lipid Bilayers; D008274:Magnesium / Q000737:chemistry*; D008565:Membrane Proteins; D009930:Organic Chemicals / Q000737:chemistry; D049294:Phospholipid Transfer Proteins
chemical_list: D000838:Anions; D002352:Carrier Proteins; D007476:Ionophores; D008051:Lipid Bilayers; D008565:Membrane Proteins; D009930:Organic Chemicals; D049294:Phospholipid Transfer Proteins; D001224:Aspartic Acid; D008274:Magnesium