원문정보
초록
영어
In a previous study, we showed that Cecropin A (1-8)-Magainin 2 (1-12) hybrid peptide (CA-MA)’s analogue, Anal P5, exhibit broad-spectrum antimicrobial activity. Anal P5, designed by flexible region (positions 9, 10)-substitution, Lys-(positions 4, 8, 14, 15) and Leu- (positions 5, 6, 12, 13, 16, 17, 20) substitutions, showed an enhanced antimicrobial and antitumor activity without hemolysis. The primary objective of the present study was to gain insight into the relevant mechanisms of antimicrobial activities of Anal P5 by using flow cytometric analysis. Anal P5 exhibits strong antifungal activity in a salt concentration independent manner. In addition, Anal P5 causes significant morphological alterations of the bacterial surfaces as shown by scanning electron microscopy, supporting its antibacterial activity. Its potent antibiotic activity suggests that Anal P5 is an excellent candidate as a lead compound for the development of novel antibiotic agents.
목차
1. Introduction
2. Materials and methods
2.1. Peptide synthesis
2.2. Antibacterial activity
2.3. Antifungal activity assay
2.4. Salt-dependency test
2.5. Scanning electron microscopy (SEM)
2.6. Circular dichroism (CD) analysis
3. Results and discussion
3.1. Design and synthesis of the peptides
3.2. Antimicrobial activity
3.3. Effects of salts on antimicrobial activity
3.4. Analysis of the peptide under bacteria morphology by scanning electron microscopy
3.5. Structural analysis of peptides by CD measurements
4. Conclusions
References