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Selection of peptide inhibitors against the Pseudomonas aeruginosa MurD cell wall enzyme
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UNSPECIFIED. (2006) Selection of peptide inhibitors against the Pseudomonas aeruginosa MurD cell wall enzyme. PEPTIDES, 27 (7). pp. 1693-1700. ISSN 0196-9781
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Official URL: http://dx.doi.org/10.1016/j.peptides.2006.01.017
Abstract
The purified Pseudomonas aeruginosa cell wall biosynthesis MurD amide ligase enzyme was used to screen C-7-C and 12 mers peptides from phage display libraries using competitive biopanning approaches with the specific substrates D-glutamate and ATP. From the 60 phage-encoded peptides identified, DNA was sequenced, deduced amino acid sequences aligned and two peptides were synthesized from consensus sequences identified. The UDPN-acetylmuramyl-L-alanine MurD substrate was synthesized, purified and used to develop a spectrophotometric assay. One peptide synthesized was found to specifically inhibit ATPase activity of MurD. The IC50 value was estimated at 4 mu M for the C-7-C MurDp1 peptide. The loop conformation of MurDp1 was shown to be important for the inhibition of the UDP-N-acetylmuramyl-L-alanine:D-glutamate MurD ligase. The linear 12 mers MurD2 peptide has an IC50 value of 15 mM. A conserved amino acid motif was found between MurDp2 and the bacterial glyceraldehyde 3-phosphate dehydrogenase indicating that MurDp2 binds at a protein-protein interacting site. The approach proposed and results obtained suggest that efficient peptide inhibitors as well as protein-protein interaction domains can be identified by phage display. (c) 2006 Elsevier Inc. All rights reserved.
| Item Type: | Journal Article |
|---|---|
| Subjects: | Q Science > QD Chemistry R Medicine > RS Pharmacy and materia medica |
| Journal or Publication Title: | PEPTIDES |
| Publisher: | ELSEVIER SCIENCE INC |
| ISSN: | 0196-9781 |
| Date: | July 2006 |
| Volume: | 27 |
| Number: | 7 |
| Number of Pages: | 8 |
| Page Range: | pp. 1693-1700 |
| Identification Number: | 10.1016/j.peptides.2006.01.017 |
| Publication Status: | Published |
| URI: | http://wrap.warwick.ac.uk/id/eprint/33330 |
Data sourced from Thomson Reuters' Web of Knowledge
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