The Discovery of Penta-peptides Inhibiting the Activity of the Formylglycine-generating Enzyme and Their Potential Antibacterial Effects Against
Overview
Overview
Journal
RSC Adv
Publisher
Royal Society of Chemistry
Specialty
Chemistry
Date
2022 Jul 25
PMID
35873338
Authors
Affiliations
Affiliations
Soon will be listed here.
Abstract
The formylglycine-generating enzyme is a key regulator that converts sulfatase into an active form. Despite its key role in many diseases, enzyme activity inhibitors have not yet been reported. In this study, we investigated penta-peptide ligands for FGE activity inhibition and discovered two hit peptides. In addition, the lead peptides also showed potential antibacterial effects in a model.
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References
1.
Eberhardt J, Santos-Martins D, Tillack A, Forli S
. AutoDock Vina 1.2.0: New Docking Methods, Expanded Force Field, and Python Bindings. J Chem Inf Model. 2021; 61(8):3891-3898.
PMC: 10683950.
DOI: 10.1021/acs.jcim.1c00203.
View
2.
Cosma M, Pepe S, Annunziata I, Newbold R, Grompe M, Parenti G
. The multiple sulfatase deficiency gene encodes an essential and limiting factor for the activity of sulfatases. Cell. 2003; 113(4):445-56.
DOI: 10.1016/s0092-8674(03)00348-9.
View
3.
Takakusaki Y, Hisayasu S, Hirai Y, Shimada T
. Coexpression of formylglycine-generating enzyme is essential for synthesis and secretion of functional arylsulfatase A in a mouse model of metachromatic leukodystrophy. Hum Gene Ther. 2005; 16(8):929-36.
DOI: 10.1089/hum.2005.16.929.
View
4.
Nguyen N, Nguyen T, Pham T, Huy N, Van Bay M, Pham M
. Autodock Vina Adopts More Accurate Binding Poses but Autodock4 Forms Better Binding Affinity. J Chem Inf Model. 2019; 60(1):204-211.
DOI: 10.1021/acs.jcim.9b00778.
View
5.
Carlson B, Ballister E, Skordalakes E, King D, Breidenbach M, Gilmore S
. Function and structure of a prokaryotic formylglycine-generating enzyme. J Biol Chem. 2008; 283(29):20117-25.
PMC: 2459300.
DOI: 10.1074/jbc.M800217200.
View