Related ArticlesGlycyrrhizin-induced changes in phospholipid dynamics studied by 1H NMR and MD simulation.
Arch Biochem Biophys. 2020 Apr 18;:108368
Authors: Selyutina OY, Shelepova EA, Paramonova ED, Kichigina LA, Khalikov SS, Polyakov NE
Abstract
Phospholipid bilayer constitutes the basis of the cell membrane. Any changes in its structure and dynamics could significantly affect the properties and functions of the cell membrane and associated proteins. It could, in its turn, affect the mechanism and strength of drug-membrane interaction. Phase transitions in lipid bilayer play an important role in cell life and in transmembrane transport of ions and drug molecules. In the present study we have tried to clarify the mechanism of glycyrrhizin bioactivity by the study of its influence on the lipid dynamics and phase transition of the lipid bilayer. For this purpose, a combination of nuclear magnetic resonance (NMR) and molecular dynamic (MD) simulations was used. Glycyrrhizin is the saponin extracted from licorice root. It displays a wide spectrum of biological activity and is frequently used in traditional medicine since ancient times. Now glycyrrhizin attracts additional attention as a novel multifunctional drug delivery system. We have established that glycyrrhizin interaction with dipalmitoylphosphatidylcholine lipid bilayers leads to changes in lipid mobility and phase transition temperature. NMR and MD results demonstrated that a glycyrrhizin molecule is able to integrate into a lipid bilayer and form stable aggregates inside. We hypothesize that surface curvatures caused by local changes in the lipid composition and the presence of phase boundaries might affect the permeability of the cell membrane.
PMID: 32315654 [PubMed - as supplied by publisher]
[NMR paper] Distinct solvent- and temperature-dependent packing arrangements of anti-parallel ?-sheet polyalanines studied with solid-state 13C NMR and MD simulation.
Distinct solvent- and temperature-dependent packing arrangements of anti-parallel ?-sheet polyalanines studied with solid-state 13C NMR and MD simulation.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.rsc.org-images-entities-char_z_RSClogo.gif Related Articles Distinct solvent- and temperature-dependent packing arrangements of anti-parallel ?-sheet polyalanines studied with solid-state 13C NMR and MD simulation.
Phys Chem Chem Phys. 2017 Aug 09;19(31):20829-20838
Authors: Kametani S, Tasei Y, Nishimura A, Asakura T
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[NMR paper] Dynamics of dehaloperoxidase-hemoglobin A derived from NMR relaxation spectroscopy and molecular dynamics simulation.
Dynamics of dehaloperoxidase-hemoglobin A derived from NMR relaxation spectroscopy and molecular dynamics simulation.
Dynamics of dehaloperoxidase-hemoglobin A derived from NMR relaxation spectroscopy and molecular dynamics simulation.
J Inorg Biochem. 2018 Jan 12;181:65-73
Authors: Zhao J, Xue M, Gudanis D, Gracz H, Findenegg GH, Gdaniec Z, Franzen S
Abstract
Dehaloperoxidase-hemoglobin is the first hemoglobin identified with biologically-relevant oxidative functions, which include peroxidase, peroxygenase and oxidase...
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[NMR paper] Pressure-induced structural transition of mature HIV-1 Protease from a combined NMR/MD simulation approach.
Pressure-induced structural transition of mature HIV-1 Protease from a combined NMR/MD simulation approach.
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Proteins. 2015 Sep 18;
Authors: Roche J, Louis JM, Bax A, Best RB
Abstract
We investigate the pressure-induced structural changes in the mature human immunodeficiency virus type 1 protease dimer (HIV-1 PR), using residual dipolar coupling (RDC) measurements in a weakly oriented solution. (1) DNH RDCs...
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[NMR paper] Conformational dynamics of oligosaccharides characterized by paramagnetism-assisted NMR spectroscopy in conjunction with molecular dynamics simulation.
Conformational dynamics of oligosaccharides characterized by paramagnetism-assisted NMR spectroscopy in conjunction with molecular dynamics simulation.
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Adv Exp Med Biol. 2015;842:217-30
Authors: Zhang Y, Yamaguchi T, Satoh T, Yagi-Utsumi M, Kamiya Y,...
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Protein Dynamics from NMR Spectroscopy and MD Simulation
Protein Dynamics from NMR Spectroscopy and MD Simulation
29 January 2013
Publication year: 2013
Source:Biophysical Journal, Volume 104, Issue 2, Supplement 1</br>
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[NMR paper] Ligand-induced structural changes to maltodextrin-binding protein as studied by solut
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J Mol Biol. 2001 Jun 15;309(4):961-74
Authors: Evenäs J, Tugarinov V, Skrynnikov NR, Goto NK, Muhandiram R, Kay LE
Solution NMR studies on the physiologically relevant ligand-free and maltotriose-bound states of maltodextrin-binding protein (MBP) are presented. Together with existing data on MBP in complex with...
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11-19-2010 08:32 PM
[NMR paper] Calcium-induced refolding of the calmodulin V136G mutant studied by NMR spectroscopy:
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Biochemistry. 2000 Dec 26;39(51):15920-31
Authors: Fefeu S, Biekofsky RR, McCormick JE, Martin SR, Bayley PM, Feeney J
The Ca(2+) titration of the (15)N-labeled mutant V136G calmodulin has been monitored using (1)H-(15)N HSQC NMR spectra. Up...
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[NMR paper] Phospholipid headgroup dynamics in DOPG-d5-cytochrome c complexes as revealed by 2H a
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http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Phospholipid headgroup dynamics in DOPG-d5-cytochrome c complexes as revealed by 2H and 31P NMR: the effects of a peripheral protein on collective lipid fluctuations.
Solid State Nucl Magn Reson. 1997 Mar;8(1):55-64
Authors: Pinheiro TJ, Duer MJ, Watts A
The...
Glycyrrhizin-induced changes in phospholipid dynamics studied by 1H NMR and MD simulation.
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