Structure-antibacterial activity relationship of cecropin A derivatives.
To investigate the effect of net positive charge, alpha-helicity and hydrophobicity of the peptides on antibacterial activity, we designed three kinds of cecropin A (CA) derivatives. Compared to CA, F3 with the highest net positive charge exhibited similar or slightly weaker antibacterial activity (MIC: 3.13 approximately 6.25 microM). F1 showed lower antibacterial activity than that of F3, even though it has higher hydrophobicity and a-helicity than F3. This result indicates that the net positive charge of cecropin A-like peptides appears to be a more important factor in antibacterial activity than alpha-helicity and hydrophobicity. The two peptides F1 and F2 possessed almost similar antibacterial activity, but F2 showed very lower activity in the membrane disruption than F1, suggesting other factors are involved in the antibacterial activity of the peptides as well as peptide-lipid interaction.
Shin
Song Yub
SY
Research Center for Proteineous Materials, Chosun University, Kwangju 501-759, Korea. syshin@chosun.ac.kr
Lee
Keun Woo
KW
Kim
Yangmee
Y
Kim
Jae Il
JI
Hahm
Kyung-Soo
KS
Kang
Shin-Won
SW
D000818:Animals; D000890:Anti-Infective Agents / Q000378:metabolism*; D023181:Antimicrobial Cationic Peptides / Q000378:metabolism*; D002942:Circular Dichroism; D009036:Moths / Q000378:metabolism; D010455:Peptides / Q000378:metabolism*; D013329:Structure-Activity Relationship
D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D010455:Peptides; C031161:cecropin A