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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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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