Interactions between glycosyltransferases and 2-deoxy glycosyl derivatives of uridine simulated by molecular docking

Ilona Wandzik

Interactions between glycosyltransferases and 2-deoxy glycosyl derivatives of uridine simulated by molecular docking

Ilona Wandzik

Department of Organic Chemistry; Bioorganic Chemistry and Biotechnology (RCH/RCH2)

Research output: Contribution to journal › Article › peer-review

2 Citations (Scopus)

Abstract

The focus of the present work was to investigate interactions between 2-deoxy sugar derivatives of uridine and active sites of N- acetylglucosaminyltransferase I and β-1,4-galactosyltransferase I. The ligand-protein interactions were simulated with a docking software (GOLD). The results suggest that the synthesized compounds bind the enzyme by a similar mode as the natural substrate.

Original language	English
Pages (from-to)	735-741
Number of pages	7
Journal	Acta Poloniae Pharmaceutica - Drug Research
Volume	65
Issue number	6
Publication status	Published - 2008

Keywords

Inhibitors of glycosyltransferases
Molecular docking
Structure-based drug design

ASJC Scopus subject areas

Pharmacology
Pharmaceutical Science

Cite this

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title = "Interactions between glycosyltransferases and 2-deoxy glycosyl derivatives of uridine simulated by molecular docking",

abstract = "The focus of the present work was to investigate interactions between 2-deoxy sugar derivatives of uridine and active sites of N- acetylglucosaminyltransferase I and β-1,4-galactosyltransferase I. The ligand-protein interactions were simulated with a docking software (GOLD). The results suggest that the synthesized compounds bind the enzyme by a similar mode as the natural substrate.",

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AU - Wandzik, Ilona

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AB - The focus of the present work was to investigate interactions between 2-deoxy sugar derivatives of uridine and active sites of N- acetylglucosaminyltransferase I and β-1,4-galactosyltransferase I. The ligand-protein interactions were simulated with a docking software (GOLD). The results suggest that the synthesized compounds bind the enzyme by a similar mode as the natural substrate.

KW - Inhibitors of glycosyltransferases

KW - Molecular docking

KW - Structure-based drug design

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AN - SCOPUS:61549110486

SN - 0001-6837

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JO - Acta Poloniae Pharmaceutica - Drug Research

JF - Acta Poloniae Pharmaceutica - Drug Research

IS - 6

ER -

Interactions between glycosyltransferases and 2-deoxy glycosyl derivatives of uridine simulated by molecular docking

Abstract

Keywords

ASJC Scopus subject areas

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