| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10835708 | Peptides | 2012 | 9 Pages |
Abstract
⺠The proper hydrophobicity of antimicrobial peptides is crucial to exert the amalgamated property of LPS-neutralizing activity and prokaryotic selectivity. ⺠Analog a4-W2 showed more improved prokaryotic selectivity compared to LL-37. ⺠Analog a4-W2 displayed LPS-neutralizing activity comparable to that of LL-37. ⺠The effective site of Trp-substitution for high LPS-neutralizing activity of α-helical antimicrobial peptides is the amphipathic interface in the α-helical wheel projection.
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Authors
Yong Hai Nan, Jeong-Kyu Bang, Binu Jacob, Il-Seon Park, Song Yub Shin,