From selection to caged aptamers: identification of light-dependent ssDNA aptamers targeting cytohesin.
Caged aptamers represent valuable tools for the spatiotemporal control of protein function by light. Here we describe a general route starting with the de novo selection process targeting cytohesin-1 and aiming at the synthesis of caged aptamers without the prior knowledge of detailed structural determinants of aptamer-target binding.
Strathclyde Institute for Pharmacy and Biological Sciences, University of Strathclyde, Glasgow G4 0NR, Scotland, United Kingdom. gunter.mayer@strath.ac.uk
Günter
G
Mayer
Andrea
A
Lohberger
Sabine
S
Butzen
Monika
M
Pofahl
Michael
M
Blind
Alexander
A
Heckel
D052157:Aptamers, Nucleotide / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D001483:Base Sequence; D001665:Binding Sites; D004277:DNA, Single-Stranded / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D020662:Guanine Nucleotide Exchange Factors / Q000037:antagonists & inhibitors* / Q000737:chemistry; D008027:Light; D008969:Molecular Sequence Data; D013329:Structure-Activity Relationship
D052157:Aptamers, Nucleotide; D004277:DNA, Single-Stranded; D020662:Guanine Nucleotide Exchange Factors; C100723:cytohesin-1