Bibliographic Details
| Title: |
Identification and Characterisation of the Antimicrobial Peptide, Phylloseptin-PT, from the Skin Secretion of Phyllomedusa tarsius, and Comparison of Activity with Designed, Cationicity-Enhanced Analogues and Diastereomers |
| Authors: |
Yitian Gao, Di Wu, Xinping Xi, Yue Wu, Chengbang Ma, Mei Zhou, Lei Wang, Mu Yang, Tianbao Chen, Chris Shaw |
| Source: |
Molecules, Vol 21, Iss 12, p 1667 (2016) |
| Publisher Information: |
MDPI AG, 2016. |
| Publication Year: |
2016 |
| Collection: |
LCC:Organic chemistry |
| Subject Terms: |
antimicrobial peptide, phylloseptin, stability, diastereomer, modification, Organic chemistry, QD241-441 |
| More Details: |
Antimicrobial peptides belonging to the phylloseptin family are mainly found in phyllomedusine frogs. These peptides not only possess potent antimicrobial activity but exhibit low toxicity against eukaryotic cells. Therefore, they are considered as promising drug candidates for a number of diseases. In a recent study, potent antimicrobial activity was correlated with the conserved structures and cationic amphiphilic characteristics of members of this peptide family. A phylloseptin peptide precursor was discovered here in the skin secretion of Phyllomedusa tarsius and the mature peptide was validated by MS/MS sequencing, and was subsequently named phylloseptin-PT. The chemically-synthesized and purified phylloseptin-PT displayed activity against Staphylococcus aureus and Candida albicans. Nevertheless, a range of cationicity-enhanced peptide analogues of phylloseptin-PT, which contained amino acid substitutions at specific sites, exhibited significant increases in antimicrobial activity compared to native phylloseptin-PT. In addition, alternative conformers which were designed and chemically-synthesized with d-lysine, showed potent antimicrobial activity and enhanced bioavailability. These data indicate that phylloseptins may represent potential candidates for next-generation antibiotics. Thus, rational design through modification of natural antimicrobial peptide templates could provide an accelerated path to overcoming obstacles en-route to their possible clinical applications. |
| Document Type: |
article |
| File Description: |
electronic resource |
| Language: |
English |
| ISSN: |
1420-3049 |
| Relation: |
http://www.mdpi.com/1420-3049/21/12/1667; https://doaj.org/toc/1420-3049 |
| DOI: |
10.3390/molecules21121667 |
| Access URL: |
https://doaj.org/article/1b4f01c4dd0e4ce1818cee161ae7d552 |
| Accession Number: |
edsdoj.1b4f01c4dd0e4ce1818cee161ae7d552 |
| Database: |
Directory of Open Access Journals |
