In vivo efficacy of anuran rypsin inhibitory peptides against Staphylococcal Skin infection and the impact of peptide cyclization

Malik, U., Silva, O. N., Fensterseifer, I. C. M., Chan, A., Clark, R. J., Franco, O. L., Daly, N. L. and Craik, D. J. (2015) In vivo efficacy of anuran rypsin inhibitory peptides against Staphylococcal Skin infection and the impact of peptide cyclization. Antimicrobial Agents and Chemotherapy, 59 4: 2113-2121. doi:10.1128/AAC.04324-14

Attached Files (Some files may be inaccessible until you login with your UQ eSpace credentials)
Name Description MIMEType Size Downloads
UQ355536_OA.pdf Full text (open access) application/pdf 1.13MB 0

Author Malik, U.
Silva, O. N.
Fensterseifer, I. C. M.
Chan, A.
Clark, R. J.
Franco, O. L.
Daly, N. L.
Craik, D. J.
Title In vivo efficacy of anuran rypsin inhibitory peptides against Staphylococcal Skin infection and the impact of peptide cyclization
Formatted title
In vivo efficacy of anuran rypsin inhibitory peptides against Staphylococcal Skin infection and the impact of peptide cyclization
Journal name Antimicrobial Agents and Chemotherapy   Check publisher's open access policy
ISSN 0066-4804
1098-6596
Publication date 2015-04-26
Year available 2015
Sub-type Article (original research)
DOI 10.1128/AAC.04324-14
Open Access Status File (Publisher version)
Volume 59
Issue 4
Start page 2113
End page 2121
Total pages 9
Place of publication Washington, DC, United States
Publisher American Society for Microbiology
Collection year 2016
Language eng
Formatted abstract
Staphylococcus aureus is a virulent pathogen that is responsible for a wide range of superficial and invasive infections. Its resistance to existing antimicrobial drugs is a global problem, and the development of novel antimicrobial agents is crucial. Antimicrobial peptides from natural resources offer potential as new treatments against staphylococcal infections. In the current study, we have examined the antimicrobial properties of peptides isolated from anuran skin secretions and cyclized synthetic analogues of these peptides. The structures of the peptides were elucidated by nuclear magnetic resonance (NMR) spectroscopy, revealing high structural and sequence similarity with each other and with sunflower trypsin inhibitor 1 (SFTI-1). SFTI-1 is an ultrastable cyclic peptide isolated from sunflower seeds that has subnanomolar trypsin inhibitory activity, and this scaffold offers pharmaceutically relevant characteristics. The five anuran peptides were nonhemolytic and noncytotoxic and had trypsin inhibitory activities similar to that of SFTI-1. They demonstrated weak in vitro inhibitory activities against S. aureus, but several had strong antibacterial activities against S. aureus in an in vivo murine wound infection model. pYR, an immunomodulatory peptide from Rana sevosa, was the most potent, with complete bacterial clearance at 3 mg · kg−1. Cyclization of the peptides improved their stability but was associated with a concomitant decrease in antimicrobial activity. In summary, these anuran peptides are promising as novel therapeutic agents for treating infections from a clinically resistant pathogen.
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2016 Collection
School of Biomedical Sciences Publications
Institute for Molecular Bioscience - Publications
 
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 1 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 1 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Thu, 02 Apr 2015, 10:37:21 EST by Katrina Garner-Moore on behalf of Institute for Molecular Bioscience