Research Article: Development and Optimization of a New Chemoenzymatic Approach for the Synthesis of Peracetylated Lactosamine (Intermediate for the Synthesis of Pharmacologically Active Compounds) Monitored by RP- HPLC Method

Date Published: June 30, 2017

Publisher: Tabriz University of Medical Sciences

Author(s): Qais Ibrahim Abualassal, Khaldun Mohammad Al Azzam, Zead Helmi Abudayeh, Loay Khaled Hassouneh.


Purpose: To describe a chemoenzymatic approach joining an enzymatic regioselective hydrolysis of peracetylated N-acetyl-α-D-glucosamine (A) with a mild controlled acyl relocation which resulted 2-acetamido-2 deoxy-1,3,6-tri-O-acetyl-α-D-glucopyranose (1B).

Partial Text

Carbohydrates are viewed as a key part in various biological processes. Given their differing difficulty in all cells, it is not surprising that glycans have various assorted part in different physiological processes. The physiological processes are made out of sophisticated multi-cell living organism form. Honestly, a generous number of bioactive compounds are glycosylated and the sugar moiety is considered as a key for their bioactivity.1 Of them, glycoproteins found in cell–cell recognition of various pathologies are of remarkable interest.2 Actually, oligosaccharides found in glycoproteins are recognized by lectin receptors, the key part for carbohydrate-mediated recognition actions.3 For example, lacto oligosaccharides series are incorporated into a couple of structures with high biological concern (e.g., glycolipids and glycoproteins) (Figure 1).4-6

An efficient chemoenzymatic procedure in order to optimize the preparation of PL 3 containing acetyl ester as extraordinary protecting group is presented herein. Compound B is a significant intermediate for the synthesis of pharmacologically active compound (e.g., complex oligosaccharides for biochemical, biophysical, or biological examinations and so on).27 Immobilized lipase from CRGL has been contrasted and the immobilized ACEXE from Bacillus pumilus, with regard to their exploitation in biotransformation of PL 1. CRGL was immobilized on two diverse solid supports, to be specific; OSCL, and DSEOD including hydrophobic adsorption. While ACEXE was covalently linked to the matrix by means of oxirane-groups sepabeads. The hydrolysis of A which catalyzed by CRGL affirmed that the performance of the immobilized enzyme is strongly affected by the kind of support. Lipase immobilized on DSEOD was more active and regioselective than the lipase immobilized on OSCL, producing 1A in 98% at 100% of conversion, and 27% at 75% of conversion of A, respectively.

This work was funded by Drug Sciences Department, Pavia University, Italy.

Not applicable.

The authors declare no conflict of interests.




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