Molecular mechanism of vSGLT inhibition by gneyulin reveals antiseptic properties against multidrug-resistant gram-negative bacteria.
Antisepsis
/ methods
Binding Sites
Drug Resistance, Multiple, Bacterial
/ drug effects
Gram-Negative Bacteria
/ drug effects
Humans
Ligands
Models, Molecular
Protein Binding
Protein Conformation
Quantitative Structure-Activity Relationship
Sodium-Glucose Transport Proteins
/ antagonists & inhibitors
Stilbenes
/ chemistry
Vibrio parahaemolyticus
/ metabolism
Aseptic agents
Bacterial resistance
Multidrug-resistant gram-negative microorganisms
vSGLT glucose transporter inhibition
Journal
Journal of molecular modeling
ISSN: 0948-5023
Titre abrégé: J Mol Model
Pays: Germany
ID NLM: 9806569
Informations de publication
Date de publication:
11 Jun 2019
11 Jun 2019
Historique:
received:
30
10
2018
accepted:
22
05
2019
entrez:
13
6
2019
pubmed:
13
6
2019
medline:
18
12
2019
Statut:
epublish
Résumé
Faced with the worldwide spread of multidrug-resistant (MDR) bacterial strains, together with a lack of any appropriate treatment, urgent steps to combat infectious diseases should be taken. Usually, bacterial components are studied to understand, by analogy, the functioning of human proteins. However, molecular data from bacteria gathered over the past decades provide a sound basis for the search for novel approaches in medical care. With this current work, we want to direct attention to inhibition of the vSGLT glucose transporter from Vibrio parahaemolyticus belonging to the sodium solute symporter (SSS) family, to block sugar transport into the bacterial cell and, as a consequence, to limit its growth. Potential bacteriostatic properties can be drawn from commercially available drugs developed for human diseases. This goal can also be reached with natural components from traditional herbal medicine. The presented data from the numerical analysis of 44 known inhibitors of sodium glucose symporters shed light on potential novel approaches in fighting Gram-negative multidrug-resistant microorganisms. Graphical abstract Molecular view on vSGLT channel inhibition by gneyulin B, the compound of natural origin.
Identifiants
pubmed: 31187300
doi: 10.1007/s00894-019-4073-9
pii: 10.1007/s00894-019-4073-9
doi:
Substances chimiques
Ligands
0
Sodium-Glucose Transport Proteins
0
Stilbenes
0
gneyulin B
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
186Subventions
Organisme : Narodowe Centrum Nauki
ID : 2015/19/B/NZ7/02380
Organisme : Fundacja na rzecz Nauki Polskiej
ID : HOMING PLUS/2013-8/6
Organisme : Wroclawskie Centrum Sieciowo-Superkomputerowe, Politechnika Wroclawska
ID : 274
Références
J Biol Chem. 2000 Aug 18;275(33):25711-6
pubmed: 10835424
J Biol Chem. 2000 Aug 25;275(34):25959-64
pubmed: 10852908
Physiology (Bethesda). 2004 Dec;19:370-6
pubmed: 15546855
Diabetes Metab Res Rev. 2005 Jan-Feb;21(1):31-8
pubmed: 15624123
J Comput Chem. 2005 Dec;26(16):1781-802
pubmed: 16222654
J Comput Chem. 2008 Aug;29(11):1859-65
pubmed: 18351591
Science. 2008 Aug 8;321(5890):810-4
pubmed: 18599740
J Comput Chem. 2010 Jan 30;31(2):455-61
pubmed: 19499576
J Comput Chem. 2010 Mar;31(4):671-90
pubmed: 19575467
J Nat Prod. 2010 Apr 23;73(4):763-7
pubmed: 20192242
Nature. 2010 Dec 16;468(7326):988-91
pubmed: 21131949
Cell Biochem Biophys. 2012 Jun;63(2):151-8
pubmed: 22383112
Curr Protoc Bioinformatics. 2014 Sep 08;47:5.6.1-32
pubmed: 25199792
Biochimie. 2015 Aug;115:187-93
pubmed: 26086341
Molecules. 2016 Aug 27;21(9):
pubmed: 27618891
Molecules. 2017 Nov 22;22(11):null
pubmed: 29165360
Biochim Biophys Acta. 1994 Jun 29;1197(2):133-66
pubmed: 8031825