Combined Approach of NMR and Molecular Dynamics within a biphasic Membrane Mimetic: Conformation and Orientation of the Bradykinin Antagonist Hoe 140

1994 ◽  
Vol 116 (17) ◽  
pp. 7532-7540 ◽  
Author(s):  
Wolfgang Guba ◽  
Rainer Haessner ◽  
Gerd Breipohl ◽  
Stefan Henke ◽  
Jochen Knolle ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Combined Approach ◽  
Bradykinin Antagonist ◽  
Membrane Mimetic ◽  
Hoe 140

Interaction of bombolitin II with a membrane-mimetic environment: an NMR and molecular dynamics simulation approach

2002 ◽  
Vol 101-102 ◽  
pp. 577-591 ◽  
Author(s):  
Luca Monticelli ◽  
Davide Pedini ◽  
Elisabetta Schievano ◽  
Stefano Mammi ◽  
Evaristo Peggion
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulation ◽  
Dynamics Simulation ◽  
Simulation Approach ◽  
Membrane Mimetic

The effect of bradykinin and the bradykinin antagonist Hoe 140 on kinematic parameters of human spermatozoa

1996 ◽  
Vol 19 (3) ◽  
pp. 143-149 ◽  
Author(s):  
C. H. YEUNG ◽  
B. SPIER ◽  
T. G. COOPER ◽  
P. NACKE ◽  
E. NIESCHLAG
Keyword(s):  
Human Spermatozoa ◽  
Kinematic Parameters ◽  
Bradykinin Antagonist ◽  
Hoe 140

scholarly journals Hoe 140 a new potent and long acting bradykinin-antagonist: in vivo studies

1991 ◽  
Vol 102 (3) ◽  
pp. 774-777 ◽  
Author(s):  
K. Wirth ◽  
F.J. Hock ◽  
U. Albus ◽  
W. Linz ◽  
H.G. Alpermann ◽  
...  
Keyword(s):  
In Vivo Studies ◽  
Bradykinin Antagonist ◽  
Hoe 140 ◽  
Long Acting

scholarly journals Кинетика ранних стадий распада в разбавленном ОЦК-сплаве Fe-Сu-Ni-Al: MC + MD-моделирование

2019 ◽  
Vol 61 (4) ◽  
pp. 724
Author(s):  
И.Н. Карькин ◽  
Л.Е. Карькина ◽  
Ю.Н. Горностырев ◽  
А.П. Коржавый
Keyword(s):  
Molecular Dynamics ◽  
Monte Carlo ◽  
Surface Layer ◽  
Molecular Dynamics Simulation ◽  
Structural Features ◽  
Al Alloys ◽  
Decomposition Kinetics ◽  
Dynamics Simulation ◽  
Combined Approach ◽  
Cu Nanoparticles

AbstractA combined approach including the Monte Carlo and molecular-dynamics simulation, decomposition kinetics and segregation formation in the multicomponent low-alloy Fe–1.5Cu–2Ni–1.5Al (at %) alloy is studied. It is shown that the formation of Cu nanoparticles surface-enriched with Ni and Al (coprecipitation mode) includes several stages: (i) the formation of clusters consisting of several Cu atoms, (ii) their enrichment with Ni and Al atoms, and (iii) redistribution of Ni and Al atoms with the formation of a surface layer providing stabilization of Cu nanoparticles. Observed structural features of segregations and their stability in Fe–Cu–Ni–Al alloys is discussed.

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.

Sign in / Sign up

Export Citation Format

Share Document