Antibiotic Activity of Reversed Peptides of A- Helical Antimicrobial Peptide, P18

Author(s): Si-Hyung Lee, Dong Gun Lee, Sung-Tae Yang, Yangmee Kim, Jae Il. Kim, Kyung-Soo Hahm, Song Yub Shin.

Journal Name: Protein & Peptide Letters

Volume 9 , Issue 5 , 2002

Become EABM
Become Reviewer

Abstract:

P18 (KWKLFKKIPKFLHLAKKF-NH2), an α-helical antimicrobial peptide designed from cecropin Amagainin 2 hybrid, was known to have potent antimicrobial activity against bacteria as well as fungi without hemolytic activity. To find the peptides comparable or superior to the antimicrobial activity of P18, the two reversed peptides (Rev-1 and Rev-2) of P18 were designed and synthesized. These peptides were found to have similar antimicrobial activity against bacterial and fungal cells without hemolytic activity as compared with P18. Furthermore, a reversed peptide, Rev-2 was shown to have a two-fold higher activity in killing some bacterial cells than P18. Therefore, these results suggested that Rev-2 peptide seems to be an excellent candidate for developing novel peptide antibiotics.

Keywords: P18, antimicrobial peptide, reversed peptide, antimicrobial activity, hemolytic activity

Rights & PermissionsPrintExport Cite as


Article Details

VOLUME: 9
ISSUE: 5
Year: 2002
Page: [395 - 402]
Pages: 8
DOI: 10.2174/0929866023408535
Price: $58

Article Metrics

PDF: 6