Chiral stationary phase based on a biostable L-RNA aptamer.
An immobilized anti-L-arginine d-RNA aptamer, used as a target-specific chiral stationary phase (CSP), was found to be very quickly degraded by RNases under usual chromatographic utilization and storage. To overcome this severe limitation for a practical use, a CSP based on the L-RNA aptamer, that is, the mirror image of the D-RNA aptamer, was created. It was shown that this mirror-image approach was a very simple and powerful strategy to develop a highly stable stationary phase due to the intrinsic insensitivity of l-RNA to the RNase degradation. In addition, such an approach allowed one to reverse the enantiomer elution order relative to that obtained with the corresponding d-RNA CSP.
Brumbt
Agnès
A
Département de Pharmacochimie Moléculaire UMR 5063 CNRS, Institut de Chimie Moléculaire de Grenoble FR 2607, Université Joseph Fourier, UFR de Pharmacie de Grenoble, Avenue de Verdun, 38240 Meylan, France.
Ravelet
Corinne
C
Grosset
Catherine
C
Ravel
Anne
A
Villet
Annick
A
Peyrin
Eric
E
D052157:Aptamers, Nucleotide / Q000737:chemistry* / Q000378:metabolism*; D001120:Arginine / Q000302:isolation & purification* / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry; D001710:Biotin / Q000031:analogs & derivatives / Q000737:chemistry; D002623:Chemistry Techniques, Analytical / Q000295:instrumentation / Q000379:methods*; D020871:RNA Stability; D012260:Ribonucleases / Q000378:metabolism; D013237:Stereoisomerism
D052157:Aptamers, Nucleotide; D001426:Bacterial Proteins; C066114:biotin-streptavidin complex; D001710:Biotin; D001120:Arginine; D012260:Ribonucleases