Abstract
By using short linear antimicrobial peptides as a model system, the effect of peptide charge on the specificity between Candida albicans (fungi) and Gram-positive bacteria was investigated. In a present study, we added and/or deleted lysine residue(s) at the C-terminal and/or N-terminal end(s) of an antimicrobial peptide (KKVVFKVKFK-NH2) and synthesized the peptides that had similar α helical structures in a lipid membrane mimic condition. The increase of peptide charge improved antifungal activity without the change of antibacterial activity. Structure-activity relationship study about the peptides revealed that the net positive charge must play an important role in the specificity between C. albicans and Gram-positive bacteria and the increase of the net positive charge without the moderate change of secondary structure could improve activity for C. albicans rather than Gram-positive bacteria.
| Original language | English |
|---|---|
| Pages (from-to) | 1669-1674 |
| Number of pages | 6 |
| Journal | Peptides |
| Volume | 22 |
| Issue number | 10 |
| DOIs | |
| State | Published - 2001 |
| Externally published | Yes |
Funding
This work was supported in part by grant from Inha University (#21352).
Keywords
- Antibacterial peptide
- Hydrophobicity
- Net positive charge
- α-helical structure