title: Inclusion of thiamine diphosphate and S-adenosylmethionine at their chemically active sites.
abstract: [structure: see text] Molecular clips functionalized by phosphonate or phosphate groups bind thiamine diphosphate (TPP) and S-adenosylmethionine (SAM) with high affinity in water; both sulfur-based cofactors transfer organic groups to biomolecules. For TPP, various analytical tools point toward a simultaneous insertion of both heterocyclic rings into the electron-rich clip cavity. Similarly, SAM is also embedded with its sulfonium moiety inside the receptor cavity. This paves the way for enzyme models and direct interference with enzymatic processes.
authors.affiliation: Department of Chemistry, University of Marburg, Hans-Meerwein-Strasse, 35032 Marburg, Germany. schradet@staff.uni-marburg.de
authors.forename: Thomas
authors.initials: T
authors.lastname: Schrader
authors.forename: Michael
authors.initials: M
authors.lastname: Fokkens
authors.forename: Frank-Gerrit
authors.initials: FG
authors.lastname: Klärner
authors.forename: Jolanta
authors.initials: J
authors.lastname: Polkowska
authors.forename: Frank
authors.initials: F
authors.lastname: Bastkowski
mesh_terms: D001665:Binding Sites; D046911:Macromolecular Substances / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008968:Molecular Conformation; D012436:S-Adenosylmethionine / Q000737:chemistry*; D012995:Solubility; D013835:Thiamine Pyrophosphate / Q000737:chemistry*; D014867:Water
chemical_list: D046911:Macromolecular Substances; D014867:Water; D012436:S-Adenosylmethionine; D013835:Thiamine Pyrophosphate