Designed low amphipathic peptides with α-helical propensity exhibiting antimicrobial activity via a lipid domain formation mechanism

Peptides ◽  
2010 ◽  
Vol 31 (5) ◽  
pp. 794-805 ◽  
Author(s):  
Naoki Yamamoto ◽  
Atsuo Tamura
Keyword(s):  
Antimicrobial Activity ◽  
Formation Mechanism ◽  
Domain Formation ◽  
Amphipathic Peptides ◽  
Lipid Domain

scholarly journals Ternary Lipid Domain Formation using Atomistic Molecular Dynamics Simulations

2013 ◽  
Vol 104 (2) ◽  
pp. 591a
Author(s):  
Alexander W. Chen ◽  
W.F. Drew Bennet ◽  
Tsjerk A. Wassenaar ◽  
D. Peter Tieleman
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulations ◽  
Domain Formation ◽  
Lipid Domain ◽  
Dynamics Simulations

scholarly journals Lipid domain formation and membrane shaping by C24-ceramide

2020 ◽  
Vol 1862 (10) ◽  
pp. 183400
Author(s):  
A.E. Ventura ◽  
A.R.P. Varela ◽  
T. Dingjan ◽  
T.C.B. Santos ◽  
A. Fedorov ◽  
...  
Keyword(s):  
Domain Formation ◽  
Lipid Domain

Effect of Proline in Basic and α-Helical Amphipathic Peptides on Acidic Liposomes and Their Antimicrobial Activity

1989 ◽  
Vol 18 (4) ◽  
pp. 599-602 ◽  
Author(s):  
Sannamu Lee ◽  
Nam Gyu Park ◽  
Tamaki Kato ◽  
Haruhiko Aoyagi ◽  
Tetsuo Kato
Keyword(s):  
Antimicrobial Activity ◽  
Amphipathic Peptides

scholarly journals The Effect of Transmembrane Protein Shape on Surrounding Lipid Domain Formation by Wetting

Biomolecules ◽  
2019 ◽  
Vol 9 (11) ◽  
pp. 729 ◽  
Author(s):  
Molotkovsky ◽  
Galimzyanov ◽  
Batishchev ◽  
Akimov
Keyword(s):  
Phase Separation ◽  
Transmembrane Protein ◽  
Lipid Phase ◽  
Lipid Domains ◽  
Domain Formation ◽  
Cellular Membranes ◽  
Lipid Domain ◽  
Liquid Ordered ◽  
Lipid Environment ◽  
Protein Shape

Signal transduction through cellular membranes requires the highly specific and coordinated work of specialized proteins. Proper functioning of these proteins is provided by an interplay between them and the lipid environment. Liquid-ordered lipid domains are believed to be important players here, however, it is still unclear whether conditions for a phase separation required for lipid domain formation exist in cellular membranes. Moreover, membrane leaflets are compositionally asymmetric, that could be an obstacle for the formation of symmetric domains spanning the lipid bilayer. We theoretically show that the presence of protein in the membrane leads to the formation of a stable liquid-ordered lipid phase around it by the mechanism of protein wetting by lipids, even in the absence of conditions necessary for the global phase separation in the membrane. Moreover, we show that protein shape plays a crucial role in this process, and protein conformational rearrangement can lead to changes in the size and characteristics of surrounding lipid domains.

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