Interaction of statins with phospholipid bilayers studied by solid-state NMR spectroscopy.


Journal

Biochimica et biophysica acta. Biomembranes
ISSN: 1879-2642
Titre abrégé: Biochim Biophys Acta Biomembr
Pays: Netherlands
ID NLM: 101731713

Informations de publication

Date de publication:
01 03 2019
Historique:
received: 20 07 2018
revised: 23 11 2018
accepted: 18 12 2018
pubmed: 24 12 2018
medline: 5 11 2019
entrez: 23 12 2018
Statut: ppublish

Résumé

Statins are drugs that specifically inhibit the enzyme HMG-CoA reductase and thereby reduce the concentration of low-density lipoprotein cholesterol, which represents a well-established risk factor for the development of atherosclerosis. The results of several clinical trials have shown that there are important intermolecular differences responsible for the broader pharmacologic actions of statins, even beyond HMG-CoA reductase inhibition. According to one hypothesis, the biological effects exerted by these compounds depend on their localization in the cellular membrane. The aim of the current work was to study the interactions of different statins with phospholipid membranes and to investigate their influence on the membrane structure and dynamics using various solid-state NMR techniques. Using

Identifiants

pubmed: 30578770
pii: S0005-2736(18)30363-8
doi: 10.1016/j.bbamem.2018.12.013
pii:
doi:

Substances chimiques

Hydroxymethylglutaryl-CoA Reductase Inhibitors 0
Lipid Bilayers 0
Phosphatidylcholines 0
Phospholipids 0
Fluvastatin 4L066368AS
Lovastatin 9LHU78OQFD
Simvastatin AGG2FN16EV
Pravastatin KXO2KT9N0G
1-palmitoyl-2-oleoylphosphatidylcholine TE895536Y5

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

584-593

Informations de copyright

Copyright © 2018 Elsevier B.V. All rights reserved.

Auteurs

Leisan F Galiullina (LF)

Kazan (Volga Region) Federal University, 18 Kremlevskaya St., 420008 Kazan, Russian Federation.

Holger A Scheidt (HA)

Institute for Medical Physics and Biophysics, Leipzig University, Härtelstr. 16-18, D-04107 Leipzig, Germany. Electronic address: holger.scheidt@medizin.uni-leipzig.de.

Daniel Huster (D)

Institute for Medical Physics and Biophysics, Leipzig University, Härtelstr. 16-18, D-04107 Leipzig, Germany.

Albert Aganov (A)

Kazan (Volga Region) Federal University, 18 Kremlevskaya St., 420008 Kazan, Russian Federation.

Vladimir Klochkov (V)

Kazan (Volga Region) Federal University, 18 Kremlevskaya St., 420008 Kazan, Russian Federation.

Articles similaires

Humans Peripheral Arterial Disease Retrospective Studies Male Female
Fucosyltransferases Drug Repositioning Molecular Docking Simulation Molecular Dynamics Simulation Humans
Nitriles Tensile Strength Materials Testing Gloves, Protective Product Packaging

The conformational landscape of fold-switcher KaiB is tuned to the circadian rhythm timescale.

Hannah K Wayment-Steele, Renee Otten, Warintra Pitsawong et al.
1.00
Rhodobacter sphaeroides Bacterial Proteins Circadian Rhythm Protein Folding Protein Conformation

Classifications MeSH