scholarly journals Easy Strategy To Increase Salt Resistance of Antimicrobial Peptides

2011 ◽  
Vol 55 (10) ◽  
pp. 4918-4921 ◽  
Author(s):  
Hui-Yuan Yu ◽  
Chih-Hsiung Tu ◽  
Bak-Sau Yip ◽  
Heng-Li Chen ◽  
Hsi-Tsung Cheng ◽  
...  

ABSTRACTThe efficacies of many antimicrobial peptides are greatly reduced under high salt concentrations, limiting their development as pharmaceutical compounds. Here, we describe an easy strategy to increase salt resistance of antimicrobial peptides by replacing tryptophan or histidine residues with the bulky amino acids β-naphthylalanine and β-(4,4′-biphenyl)alanine. The activities of the salt-sensitive peptide P-113 were diminished at high salt concentrations, whereas the activities of its β-naphthylalanine and β-(4,4′-biphenyl)alanine-substituted variant were less affected.

2020 ◽  
Vol 21 (18) ◽  
pp. 6810
Author(s):  
Hung-Lun Chu ◽  
Ya-Han Chih ◽  
Kuang-Li Peng ◽  
Chih-Lung Wu ◽  
Hui-Yuan Yu ◽  
...  

A strategy was described to design antimicrobial peptides (AMPs) with enhanced salt resistance and antiendotoxin activities by linking two helical AMPs with the Ala-Gly-Pro (AGP) hinge. Among the designed peptides, KR12AGPWR6 demonstrated the best antimicrobial activities even in high salt conditions (NaCl ~300 mM) and possessed the strongest antiendotoxin activities. These activities may be related to hydrophobicity, membrane-permeability, and α-helical content of the peptide. Amino acids of the C-terminal helices were found to affect the peptide-induced permeabilization of LUVs, the α-helicity of the designed peptides under various LUVs, and the LPS aggregation and size alternation. A possible model was proposed to explain the mechanism of LPS neutralization by the designed peptides. These findings could provide a new approach for designing AMPs with enhanced salt resistance and antiendotoxin activities for potential therapeutic applications.


2013 ◽  
Vol 57 (8) ◽  
pp. 4050-4052 ◽  
Author(s):  
Hung-Lun Chu ◽  
Hui-Yuan Yu ◽  
Bak-Sau Yip ◽  
Ya-Han Chih ◽  
Chong-Wen Liang ◽  
...  

ABSTRACTThe efficacies of many antimicrobial peptides are greatly reduced under high salt concentrations, therefore limiting their use as pharmaceutical agents. Here, we describe a strategy to boost salt resistance and serum stability of short antimicrobial peptides by adding the nonnatural bulky amino acid β-naphthylalanine to their termini. The activities of the short salt-sensitive tryptophan-rich peptide S1 were diminished at high salt concentrations, whereas the activities of its β-naphthylalanine end-tagged variants were less affected.


Author(s):  
Xingliang Li ◽  
Minji Li ◽  
Beibei Zhou ◽  
Yuzhang Yang ◽  
Jia Zhou ◽  
...  

ChemBioChem ◽  
2020 ◽  
Vol 21 (17) ◽  
pp. 2518-2526
Author(s):  
Uttam Ghosh ◽  
Isha Soni ◽  
Grace Kaul ◽  
Priyanka Trivedi ◽  
Vinita Chaturvedi ◽  
...  

ChemInform ◽  
2011 ◽  
Vol 42 (7) ◽  
pp. no-no
Author(s):  
James Ternois ◽  
Laurent Ferron ◽  
Gerard Coquerel ◽  
Guillen Guillen

2018 ◽  
Vol 29 (7) ◽  
pp. 1163-1166 ◽  
Author(s):  
Ming Kai ◽  
Wei Zhang ◽  
Huan Xie ◽  
Liwei Liu ◽  
Sujie Huang ◽  
...  

Author(s):  
Amanda L. ◽  
David Klapper ◽  
Antoine H. ◽  
Jayendra B. ◽  
Richard Borschel ◽  
...  

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