Abstract
The antimicrobial peptide KLKLLLLLKLK-NH2 was developed based on sapesin B, and synthesized using D-amino acids. Biochemical properties of the D-form and L-form KLKLLLLLKLK-NH2 peptides were compared. In order to limit the effects due to bacterial resistance to proteolysis, antimicrobial activities of the peptides were evaluated after short-term exposure to bacteria. D-form KLKLLLLLKLK-NH2 exhibited higher antimicrobial activities than L-form KLKLLLLLKLK-NH2 against bacteria, including Staphylococcus aureus and Escherichia coli. In contrast, both the D-form and L-form of other antimicrobial peptides, including Mastoparan M and Temporin A, exhibited similar antimicrobial activities. Both the D-form KLKLLLLLKLK-NH2 and L-form KLKLLLLLKLK-NH2 peptides preferentially disrupted S. aureus-mimetic liposomes over mammalian-mimetic liposomes. Furthermore, the D-form KLKLLLLLKLK-NH2 increased the membrane permeability of S. aureus more than the L-form KLKLLLLLKLK-NH2. Thus suggesting that the enhanced antimicrobial activity of the D-form was likely due to its interaction with bacterial cell wall components. S. aureus peptidoglycan preferentially inhibited the antimicrobial activity of the D-form KLKLLLLLKLK-NH2 relative to the L-form. Furthermore, the D-form KLKLLLLLKLK-NH2 showed higher affinity for S. aureus peptidoglycan than the L-form. Taken together, these results indicate that the D-form KLKLLLLLKLK-NH2 peptide has higher antimicrobial activity than the L-form via a specific association with bacterial cell wall components, including peptidoglycan.
Highlights
The antimicrobial peptide KLKLLLLLKLK-NH2 was developed based on sapesin B, and synthesized using D-amino acids
In order to further examine the antimicrobial properties of D-form KLKLLLLLKLK-NH2, we determined the minimum inhibitory concentrations (MICs) of the peptides against S. aureus, Escherichia coli, and Candida albicans
The MIC of D-forms and L-forms of Mastoparan M, Kn2–7, and Temporin A against S. aureus (Table 2) were similar. These observations indicate that KLKLLLLLKLK-NH2 and its related peptide KLKLLLKLK-NH2 are unique because these D-form peptides display lower MICs against S. aureus than their L-forms
Summary
The antimicrobial peptide KLKLLLLLKLK-NH2 was developed based on sapesin B, and synthesized using D-amino acids. The D-form KLKLLLLLKLK-NH2 showed higher affinity for S. aureus peptidoglycan than the L-form Taken together, these results indicate that the D-form KLKLLLLLKLK-NH2 peptide has higher antimicrobial activity than the L-form via a specific association with bacterial cell wall components, including peptidoglycan. Antimicrobial peptides may be synthesized from D-amino acids instead of L-amino acids, which makes them resistant to proteolytic degradation Both D-form and L-form antimicrobial peptides showed similar antimicrobial activity[8,9,10,11,12]. Sapecin B is an antimicrobial peptide that was originally isolated from the culture medium of an embryonic cell line, NIH-Sape-4, derived from Sarcophaga peregrine (flesh fly) It displays potent activity against Gram-positive bacteria[13]. D-form KLKLLLLLKLK-NH2 showed higher affinity for bacterial cell wall components, such as peptidoglycan, than its L-form. The enhanced antimicrobial activity of the D-form KLKLLLLLKLK-NH2 relative to its L-form is due to direct interactions with bacterial cell surface components
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
