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Open AccessArticle

Antimicrobial Peptides with Enhanced Salt Resistance and Antiendotoxin Properties

1
Institute of Biotechnology and Department of Medical Science, National Tsing Hua University, Hsinchu 300, Taiwan
2
Department of Radiology, Harbor-UCLA Medical Center, 1000 West Carson Street, Torrance, CA 90509, USA
*
Author to whom correspondence should be addressed.
These authors contributed equally to this paper.
Int. J. Mol. Sci. 2020, 21(18), 6810; https://doi.org/10.3390/ijms21186810
Received: 13 August 2020 / Revised: 8 September 2020 / Accepted: 12 September 2020 / Published: 16 September 2020
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. View Full-Text
Keywords: antimicrobial peptide; salt resistance; lipopolysaccharide; antiendotoxin; cecropin-like antimicrobial peptide; salt resistance; lipopolysaccharide; antiendotoxin; cecropin-like
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MDPI and ACS Style

Chu, H.-L.; Chih, Y.-H.; Peng, K.-L.; Wu, C.-L.; Yu, H.-Y.; Cheng, D.; Chou, Y.-T.; Cheng, J.-W. Antimicrobial Peptides with Enhanced Salt Resistance and Antiendotoxin Properties. Int. J. Mol. Sci. 2020, 21, 6810.

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