Differential regulation of protein subdomain activity with caged bivalent ligands.
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.
Mayer
Günter
G
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
Müller
Jens
J
Mack
Timo
T
Freitag
Daniel F
DF
Höver
Thomas
T
Pötzsch
Bernd
B
Heckel
Alexander
A
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
D052157:Aptamers, Nucleotide; D008024:Ligands; D009705:Nucleosides; D011506:Proteins; D013917:Thrombin