Synthetic Method for 2'-Amino-LNA Bearing Any of the Four Nucleobases via a Transglycosylation Reaction.

Org Lett

Research Unit/Immunology & Inflammation, Sohyaku. Innovative Research Division , Mitsubishi Tanabe Pharma Corporation , 1000, Kamoshida-cho , Aoba-ku , Yokohama 227-0033 , Japan.

Published: April 2018

A transglycosylation reaction of 2'-amino-locked nucleic acid (LNA) from thymine (T) to other nucleobases adenine (A), guanine (G), and 5-methylcytosine (C) has been developed. This reaction proceeds in high yield and with high β-selectivity. The mild reaction conditions enable the coexistence of acid-labile protecting groups, including a 4,4'-dimethoxytrytyl (DMTr) group. 2'-Amino-LNAs bearing any nucleobase can now be easily synthesized.

Download full-text PDF

Source
http://dx.doi.org/10.1021/acs.orglett.8b00476DOI Listing

Publication Analysis

Top Keywords

transglycosylation reaction
8
synthetic method
4
method 2'-amino-lna
4
2'-amino-lna bearing
4
bearing nucleobases
4
nucleobases transglycosylation
4
reaction
4
reaction transglycosylation
4
reaction 2'-amino-locked
4
2'-amino-locked nucleic
4

Similar Publications

We investigated the transglycosylation reaction of two types of oligosaccharide acceptors, i.e., β-cyclodextrin (CD) derivatives 1 and 2 conjugated with multiple glucose (Glc) units, catalyzed by endo-β-N-acetyl-glucosaminidase from Mucor hiemalis (Endo-M) using the oligosaccharide donor sialoglycopeptide (SGP).

View Article and Find Full Text PDF

Structural elucidation and characterization of GH29A α-l-fucosidases and the effect of pH on their transglycosylation.

FEBS J

December 2024

Section for Protein Chemistry and Enzyme Technology, Department of Biotechnology and Biomedicine, DTU Bioengineering, Technical University of Denmark, Kgs. Lyngby, Denmark.

Article Synopsis
  • GH29A α-l-fucosidases are enzymes that help break down specific sugars in glycoconjugates and can also be used to create human milk oligosaccharides (HMOs) through a process called transglycosylation.
  • Researchers used bioinformatics tools and phylogenetic clustering to identify and analyze new microbial GH29A α-l-fucosidases from an underexplored group, as well as previously known enzymes, to determine their biochemical properties and behavior under different conditions.
  • The study found that transglycosylation of certain substrates was most effective at neutral to alkaline pH levels and revealed new structural insights into how these enzymes function, particularly regarding regioselectivity in product formation.
View Article and Find Full Text PDF

Action pattern of Sulfolobus O-α-glycoligase for synthesis of highly water soluble resveratrol 3,4'-α-diglucoside.

Enzyme Microb Technol

December 2024

Department of Food and Biotechnology, Korea University, Sejong 30019, Republic of Korea. Electronic address:

This study presents the enzymatic synthesis of resveratrol-3,4'-O-α-diglucoside (RDG) using a hyperactive O-α-glycoligase (MalA-D416R/Q450S) and α-glucopyranosyl fluoride as the donor substrate. The transglycosylation rate for resveratrol by MalA-D416R/Q450S was maximized in 100 mM Tris-HCl (pH 9.5) containing 20 % DMSO at 45°C.

View Article and Find Full Text PDF
Article Synopsis
  • Achieving enzymatic food processing at high substrate concentrations can boost production efficiency, but research in this area is limited.
  • The study investigates enzymatic synthesis of fructooligosaccharides (FOS) under high temperature and substrate concentration, finding that higher temperatures can help overcome issues with viscosity and solubility.
  • Improved thermostability of the enzyme at elevated sucrose concentrations enabled a 155.9% increase in transglycosylation rate and a 113.5% boost in productivity, highlighting innovative approaches for food processing in the industry.
View Article and Find Full Text PDF

Engineering a Bifunctional Fusion Purine/Pyrimidine Nucleoside Phosphorylase for the Production of Nucleoside Analogs.

Biomolecules

September 2024

Applied Biotechnology Group, Universidad Europea de Madrid, Urbanización El Bosque, Villaviciosa de Odón, 28670 Madrid, Spain.

Article Synopsis
  • * The study introduces engineered bifunctional fusion enzymes from purine nucleoside phosphorylase I (PNP I) and thymidine phosphorylase (TP), offering a more efficient one-pot synthesis method for nucleosides, as opposed to traditional multi-enzyme systems.
  • * These fusion enzymes operate well at high temperatures (60-90 °C) and specific pH levels (6-8), demonstrating strong stability and successful catalysis for various nucleoside analogs, highlighting their potential in
View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!