scholarly journals Insights into Membrane Translocation of Protegrin Antimicrobial Peptides by Multistep Molecular Dynamics Simulations

ACS Omega ◽  
2018 ◽  
Vol 3 (6) ◽  
pp. 6056-6065 ◽  
Author(s):  
Pin-Kuang Lai ◽  
Yiannis N. Kaznessis
Keyword(s):  
Molecular Dynamics ◽  
Antimicrobial Peptides ◽  
Molecular Dynamics Simulations ◽  
Membrane Translocation ◽  
Dynamics Simulations

Synergistic effects of magainin 2 and PGLa on their heterodimer formation, aggregation, and insertion into the bilayer

RSC Advances ◽  
2015 ◽  
Vol 5 (3) ◽  
pp. 2047-2055 ◽  
Author(s):  
Eol Han ◽  
Hwankyu Lee
Keyword(s):  
Molecular Dynamics ◽  
Antimicrobial Peptides ◽  
Molecular Dynamics Simulations ◽  
Lipid Bilayers ◽  
Synergistic Effects ◽  
Coarse Grained ◽  
Dynamics Simulations ◽  
Coarse Grained Molecular Dynamics

We performed coarse-grained molecular dynamics simulations of antimicrobial peptides PGLa and magainin 2 in lipid bilayers.

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.

scholarly journals Molecular Dynamics Simulations of Membrane Translocation of Dendrimers

2016 ◽  
Vol 110 (3) ◽  
pp. 571a
Author(s):  
Valreia Marquez-Miranda ◽  
Ingrid Araya-Duran ◽  
Jeffrey Comer ◽  
Maria Carolina Otero Acuna ◽  
Jonathon Canan ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulations ◽  
Membrane Translocation ◽  
Dynamics Simulations
Sign in / Sign up

Export Citation Format

Share Document