Enhancement of antimicrobial activity of neuropeptide Y by N-terminal truncation.
The activity of neuropeptide Y (NPY) against Candida albicans, which was revealed to be fungicidal, was enhanced significantly by the truncation of amino acid residues at the N terminus. The most active peptides (MICs, approximately 1 microM) were about 10-fold more potent than the intact NPY (MIC, approximately 10 microM). The enhancement was weakened by the replacement of the N terminus by negatively charged residues and/or acylation of the alpha-amino group. These results suggest that only the alpha-helical region of NPY is necessary for the antimicrobial activity and that the net charge of the peptide is important for the activity.
Shimizu
M
M
Osaka National Research Institute, AIST, Ikeda, Osaka 563-8577, Japan.
Shigeri
Y
Y
Tatsu
Y
Y
Yoshikawa
S
S
Yumoto
N
N
D000595:Amino Acid Sequence; D000935:Antifungal Agents / Q000494:pharmacology*; D002176:Candida albicans / Q000187:drug effects*; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D009478:Neuropeptide Y / Q000494:pharmacology*; D013329:Structure-Activity Relationship
D000935:Antifungal Agents; D009478:Neuropeptide Y