title: Differential regulation of protein subdomain activity with caged bivalent ligands.
abstract: Subtle change: Spatiotemporal modulation of individual protein subdomains with light as the trigger signal becomes possible by using bivalent aptamers and introducing photolabile "caging groups" to switch individual aptamer modules ON or OFF differentially. To the best of our knowledge, this is the first study to show that it is possible to modulate individual domain activity in aptamers, and thus also domain activity in proteins, with light.
authors.affiliation: Life and Medical Sciences, Program Unit Chemical Biology and Medicinal Chemistry, University of Bonn c/o Kekulé Institute for Organic Chemistry and Biochemistry, Gerhard-Domagk-Strasse 1, Bonn, Germany. gmayer@uni-bonn.de
authors.forename: Günter
authors.initials: G
authors.lastname: Mayer
authors.forename: Jens
authors.initials: J
authors.lastname: Müller
authors.forename: Timo
authors.initials: T
authors.lastname: Mack
authors.forename: Daniel F
authors.initials: DF
authors.lastname: Freitag
authors.forename: Thomas
authors.initials: T
authors.lastname: Höver
authors.forename: Bernd
authors.initials: B
authors.lastname: Pötzsch
authors.forename: Alexander
authors.initials: A
authors.lastname: Heckel
mesh_terms: D052157:Aptamers, Nucleotide / Q000737:chemistry* / Q000235:genetics / Q000494:pharmacology*; D008024:Ligands; D009154:Mutation; D009705:Nucleosides / Q000737:chemistry; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism*; D013917:Thrombin / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism
chemical_list: D052157:Aptamers, Nucleotide; D008024:Ligands; D009705:Nucleosides; D011506:Proteins; D013917:Thrombin