121058-82-0Relevant articles and documents
Methylamine Deprotection Provides Increased Yield of Oligoribonucleotides
Reddy, M. P.,Farooqui, Firdous,Hanna, Naeem B.
, p. 8929 - 8932 (1995)
Use of methylamine or methylamine/ammonium hydroxide as a cleavage and deprotection reagent for the solid phase synthesis of oligoribonucleotides has significantly increased the yield of the full length oligoribonucleotides as compared to the use of conventional ammonium hydroxide/ethanol.
A base-labile group for 2′-OH protection of ribonucleosides: A major challenge for RNA synthesis
Lavergne, Thomas,Bertrand, Jean-Remi,Vasseur, Jean-Jacques,Debart, Francoise
scheme or table, p. 9135 - 9138 (2009/10/01)
A base-labile group for 2'-OH protection of ribonucleosides was investigated. The solid support was dried by blowing argon through a DNA synthesizer and was first treated with 10% anhydrous piperidine in CH 3CN at room temperature for 15 minutes to eliminate cyanoethyl groups from phosphates. The piperidine solution was removed from the column and the solid support was washed with CH3CN. The three ammoniacal eluates were collected in a screw-capped glass vial and were left at room temperature for a further 1.5 hours to completely deprotect nucleobases and 2'-hydroxyl groups. The fully deprotected oligonucleotide was transferred to a 50 mL round-bottomed flask and isopropylamine was added to the solution before evaporation to dryness. It was observed that PivOM method provides highly pure RNA without any additional desalting step.
Synthesis of a new transition-state analog of the sialyl donor. Inhibition of sialyltransferases
Sun, Hongbin,Yang, Jingsong,Amaral, Katie E.,Horenstein, Benjamin A.
, p. 2451 - 2453 (2007/10/03)
A new class of glycosyltransferase inhibitor has been designed and synthesized. The designed inhibitors 3a/3b provide conformational mimicry of the transition state in sialyltransfer reactions. The key synthetic steps involve a Meinwald rearrangement and a palladium-catalyzed carbonylation reaction. The results of kinetic studies show that 3a/3b exhibit significant inhibition on both 2,3- and 2,6-sialytransferases.