Structural characterization of the H2O/CCl4 liquid interface using molecular dynamics simulations

2004 ◽  
pp. 81-85 ◽  
Author(s):  
N. H. Moreira ◽  
M. S. Skaf
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulations ◽  
Structural Characterization ◽  
Liquid Interface ◽  
Dynamics Simulations

scholarly journals Structural characterization of the saxitoxin-targeting APTSTX1 aptamer using optical tweezers and molecular dynamics simulations

PLoS ONE ◽  
2019 ◽  
Vol 14 (11) ◽  
pp. e0222468
Author(s):  
Nathalie Casanova-Morales ◽  
Nataniel L. Figueroa ◽  
Karol Alfaro ◽  
Felipe Montenegro ◽  
Nelson P. Barrera ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulations ◽  
Optical Tweezers ◽  
Structural Characterization ◽  
Dynamics Simulations

Structural characterization of recombinant human myoglobin isoforms by 1H and 129Xe NMR and molecular dynamics simulations

2011 ◽  
Vol 1814 (12) ◽  
pp. 1919-1929 ◽  
Author(s):  
Maristella Gussoni ◽  
Mariano Andrea Scorciapino ◽  
Alessandra Vezzoli ◽  
Roberto Anedda ◽  
Fulvia Greco ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulations ◽  
Structural Characterization ◽  
129Xe Nmr ◽  
Human Myoglobin ◽  
Dynamics Simulations

scholarly journals Structural characterization of the antimicrobial peptides myxinidin and WMR in bacterial membrane mimetic micelles and bicelles

2021 ◽  
Author(s):  
Yevhen K. Cherniavskyi ◽  
Rosario Oliva ◽  
Marco Stellato ◽  
Pompea Del Vecchio ◽  
Stefania Galdiero ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Antimicrobial Peptides ◽  
Molecular Dynamics Simulations ◽  
Lipid Bilayers ◽  
Structural Characterization ◽  
Bacterial Membrane ◽  
Membrane Composition ◽  
Membrane Mimetic ◽  
Dynamics Simulations

Antimicrobial peptides are a promising class of alternative antibiotics that interact selectively with negatively charged lipid bilayers. This paper presents the structural characterization of the antimicrobial peptides myxinidin and WMR associated with bacterial membrane mimetic micelles and bicelles by NMR, CD spectroscopy, and Molecular Dynamics simulations. Both peptides adopt a different conformation in the lipidic environment than in aqueous solution. The location of peptides in micelles and bicelles has been studied by paramagnetic relaxation enhancement experiments with paramagnetic tagged 5- and 16-doxyl stearic acid (5-/16-SASL). Multi-microsecond long molecular dynamics simulations of multiple copies of the peptides were used to gain an atomic level of detail on membrane-peptide and peptide-peptide interactions. Our results highlight an essential role of the negatively charged membrane mimetic in the structural stability of both myxinidin and WMR. The peptides localize predominantly in the membrane's headgroup region and have a noticeable membrane thinning effect on the overall bilayer structure. Myxinidin and WMR show different tendency to self-aggregate, which is also influenced by the membrane composition (DOPE/DOPG versus DOPE/DOPG/CL) and can be related to the previously observed difference in the ability of the peptides to disrupt different types of model membranes.

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