Adelaide Research & Scholarship
Please use this identifier to cite or link to this item:
https://hdl.handle.net/2440/104012
| Citations | ||
| Scopus | Web of Science® | Altmetric |
|---|---|---|
|
?
|
?
|
|
| Type: | Journal article |
| Title: | New series of BPL inhibitors to probe the ribose-binding pocket of Staphylococcus aureus biotin protein ligase |
| Author: | Feng, J. Paparella, A. Tieu, W. Heim, D. Clark, S. Hayes, A. Booker, G. Polyak, S. Abell, A. |
| Citation: | ACS Medicinal Chemistry Letters, 2016; 7(12):1068-1072 |
| Publisher: | American Chemical Society |
| Issue Date: | 2016 |
| ISSN: | 1948-5875 1948-5875 |
| Statement of Responsibility: | Jiage Feng, Ashleigh S. Paparella, William Tieu, David Heim, Sarah Clark, Andrew Hayes, Grant W. Booker Steven W. Polyak and Andrew D. Abell |
| Abstract: | Replacing the labile adenosinyl-substituted phosphoanhydride of biotinyl-5'-AMP with a N1-benzyl substituted 1,2,3-triazole gave a new truncated series of inhibitors of Staphylococcus aureus biotin protein ligase (SaBPL). The benzyl group presents to the ribose-binding pocket of SaBPL based on in silico docking. Halogenated benzyl derivatives (12t, 12u, 12w, and 12x) proved to be the most potent inhibitors of SaBPL. These derivatives inhibited the growth of S. aureus ATCC49775 and displayed low cytotoxicity against HepG2 cells. |
| Keywords: | Enzyme inhibitors; antibiotics; biotin protein ligase; Staphylococcus aureus |
| Rights: | © 2016 American Chemical Society |
| DOI: | 10.1021/acsmedchemlett.6b00248 |
| Grant ID: | http://purl.org/au-research/grants/nhmrc/1068885 |
| Published version: | http://dx.doi.org/10.1021/acsmedchemlett.6b00248 |
| Appears in Collections: | Aurora harvest 7 Chemistry and Physics publications |
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.