scholarly journals Correction to “A Potent Host Defense Peptide Triggers DNA Damage and Is Active against Multidrug-Resistant Gram-Negative Pathogens”

2020 ◽  
Vol 6 (9) ◽  
pp. 2542-2542
Author(s):  
Samuel A. Juliano ◽  
Leonardo F. Serafim ◽  
Searle S. Duay ◽  
Maria Heredia Chavez ◽  
Gaurav Sharma ◽  
...  
2020 ◽  
Vol 6 (5) ◽  
pp. 1250-1263 ◽  
Author(s):  
Samuel A. Juliano ◽  
Leonardo F. Serafim ◽  
Searle S. Duay ◽  
Maria Heredia Chavez ◽  
Gaurav Sharma ◽  
...  

2020 ◽  
Vol 8 (2) ◽  
pp. 739-745 ◽  
Author(s):  
Weinan Jiang ◽  
Ximian Xiao ◽  
Yueming Wu ◽  
Weiwei Zhang ◽  
Zihao Cong ◽  
...  

Host defense peptide mimicking peptide polymer displayed potent in vitro and in vivo antimicrobial activity against clinically isolated multidrug resistant Pseudomonas aeruginosa.


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.


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