| 초록 |
The antibacterial peptides need to develop that are non resistant to the rapid emergency of bacterial infections. Here we report that repeat of alternating polar and nonpolar residues peptides act on Gram negative and Gram positive, including multidrug resistant bacterial membranes, a rapid collapse of transmembrane potential, ability to induce membrane permeability, and cause rapid cell death. Antibacterial activity of these scrambled peptides increases until a certain balance of cationic and hydrophobicity level. Further increasing cationic and hydrophobicity in the scrambled peptide was demonstrated to correlate with peptide beta sheet and self associating ability in aqueous environment. This study was supported by IPET(Korea Institute of planning & Evaluation for Technology in Food, Agriculture, Forestry & Fisheries) Research Fund in 2009. |
