Cardiolipin prevents pore formation in phosphatidylglycerol bacterial membrane models

FEBS Letters ◽  
2021 ◽  
Author(s):  
Cristian Rocha‐Roa ◽  
Juan David Orjuela ◽  
Chad Leidy ◽  
Pilar Cossio ◽  
Camilo Aponte‐Santamaría
2013 ◽  
Vol 117 (20) ◽  
pp. 6187-6193 ◽  
Author(s):  
Marina Pinheiro ◽  
Cláudia Nunes ◽  
João M. Caio ◽  
Cristina Moiteiro ◽  
Marlene Lúcio ◽  
...  

Author(s):  
Felsis Angelene Daison ◽  
Nitheeshkumar Kumar ◽  
Siranjeevi Balakrishnan ◽  
Kavyashree Venugopal ◽  
Sangamithra Elango ◽  
...  

2021 ◽  
Vol 22 (22) ◽  
pp. 12401
Author(s):  
Tadsanee Awang ◽  
Phoom Chairatana ◽  
Ranjit Vijayan ◽  
Prapasiri Pongprayoon

Human α-defensin 5 (HD5) is a host-defense peptide exhibiting broad-spectrum antimicrobial activity. The lipopolysaccharide (LPS) layer on the Gram-negative bacterial membrane acts as a barrier to HD5 insertion. Therefore, the pore formation and binding mechanism remain unclear. Here, the binding mechanisms at five positions along the bacterial membrane axis were investigated using Molecular Dynamics. (MD) simulations. We found that HD5 initially placed at positions 1 to 3 moved up to the surface, while HD5 positioned at 4 and 5 remained within the membrane interacting with the middle and inner leaflet of the membrane, respectively. The arginines were key components for tighter binding with 3-deoxy-d-manno-octulosonic acid (KDO), phosphates of the outer and inner leaflets. KDO appeared to retard the HD5 penetration.


2017 ◽  
Vol 67 ◽  
pp. 202-212 ◽  
Author(s):  
Abirami Arasu ◽  
Venkatesh Kumaresan ◽  
Rajesh Palanisamy ◽  
Mariadhas Valan Arasu ◽  
Naif Abdullah Al-Dhabi ◽  
...  

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