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.
Osaka National Research Institute, AIST, Ikeda, Osaka 563-8577, Japan.
M
M
Shimizu
Y
Y
Shigeri
Y
Y
Tatsu
S
S
Yoshikawa
N
N
Yumoto
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