Format

Send to

Choose Destination
Int J Biol Macromol. 2019 Jul 1;132:1140-1146. doi: 10.1016/j.ijbiomac.2019.04.049. Epub 2019 Apr 10.

Lactose derivatives as potential inhibitors of pectin methylesterases.

Author information

1
EA3900-BIOPI, Biologie des Plantes et Innovation, SFR Condorcet FR CNRS 3417, Université de Picardie, 33 Rue St Leu, FR-80039 Amiens, France.
2
Laboratoire de Glycochimie, des Antimicrobiens et des Agroressources (LG2A), UMR CNRS 7378 - Institut de Chimie de Picardie FR CNRS 3085, Université de Picardie Jules Verne, FR-80039 Amiens, France.
3
Department of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA.
4
Department of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA; Department of Computer Science, Purdue University, West Lafayette, IN 47907, USA.
5
EA3900-BIOPI, Biologie des Plantes et Innovation, SFR Condorcet FR CNRS 3417, Université de Picardie, 33 Rue St Leu, FR-80039 Amiens, France. Electronic address: corinne.pau-roblot@u-picardie.fr.

Abstract

The discovery of molecules that can inhibit the action of phytopathogens is essential to find alternative to current pesticides. Pectin methylesterases (PME), enzymes that fine-tune the degree of methylesterification of plant cell wall pectins, play a key role in the pathogenicity of fungi or bacteria. Here we report the synthesis of new lactoside derivatives and their analysis as potential PME inhibitors using three plants and one fungal PME. Because of its structure, abundance and reduced cost, lactose was chosen as a case study. Lactoside derivatives were obtained by TEMPO-mediated oxidation of methyl lactoside, followed by an esterification procedure. Three derivatives were synthesized: sodium (methyl-lactosid)uronate, methyl (methyl-lactosid)uronate and butyl (methyl-lactosid)uronate. The inhibition of the plant and pathogen enzyme activities by lactoside derivatives was measured in vitro, showing the importance of the substitution on lactose: methyl (methyl-lactosid)uronate was more efficient than butyl (methyl-lactosid)uronate. These results were confirmed by docking analysis showing the difference in the interaction between lactoside derivatives and PME proteins. In conclusion, this study identified novel inhibitors of pectin remodeling enzymes.

KEYWORDS:

Chemical inhibitors; Docking analysis; Lactoside derivatives; Pectin methylesterase

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center