| 초록 |
PMAP-23, which adopts a helix-to-helix structure, has potent antimicrobial activity and is a member of the cathelicidin family derived from pig myeloid. The amidation of the carboxyl terminus (C-terminus) of the antimicrobial peptide generally enhances the structural stability and antimicrobial activity or decreases cytotoxicity. The aim of this study was reveal the role of amidation in the mode of action in PMAP-23. This study results suggest that the N-terminal amidation of PMAP-23 provide structural stability and increase the cationic charge following translocation into the bacterial inner membrane. This study was supported by IPET(Korea Institute of planning & Evaluation for Technology in Food, Agriculture, Forestry & Fisheries) Research Fund in 2009. |
