Skip to content Skip to navigation
University of Warwick
  • Study
  • |
  • Research
  • |
  • Business
  • |
  • Alumni
  • |
  • News
  • |
  • About

University of Warwick
Publications service & WRAP

Highlight your research

  • WRAP
    • Home
    • Search WRAP
    • Browse by Warwick Author
    • Browse WRAP by Year
    • Browse WRAP by Subject
    • Browse WRAP by Department
    • Browse WRAP by Funder
    • Browse Theses by Department
  • Publications Service
    • Home
    • Search Publications Service
    • Browse by Warwick Author
    • Browse Publications service by Year
    • Browse Publications service by Subject
    • Browse Publications service by Department
    • Browse Publications service by Funder
  • Help & Advice
University of Warwick

The Library

  • Login
  • Admin

Selection of peptide inhibitors against the Pseudomonas aeruginosa MurD cell wall enzyme

Tools
- Tools
+ Tools

Paradis-Bleau , Catherine, Beaumont, Mélanie , Boudreault, Lydia , Lloyd, Adrian, Sanschagrina, François , Bugg, Tim and Levesquea, Roger C. (2006) Selection of peptide inhibitors against the Pseudomonas aeruginosa MurD cell wall enzyme. Peptides, Volume 27 (Number 7). pp. 1693-1700. doi:10.1016/j.peptides.2006.01.017 ISSN 0196-9781.

Research output not available from this repository.

Request-a-Copy directly from author or use local Library Get it For Me service.

Official URL: http://dx.doi.org/10.1016/j.peptides.2006.01.017

Request Changes to record.

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
Divisions: Faculty of Science, Engineering and Medicine > Science > Chemistry
Journal or Publication Title: Peptides
Publisher: Elsevier Inc
ISSN: 0196-9781
Official Date: March 2006
Dates:
DateEvent
15 December 2005Submitted
20 January 2006Updated
6 January 2006Accepted
March 2006Available
Volume: Volume 27
Number: Number 7
Number of Pages: 8
Page Range: pp. 1693-1700
DOI: 10.1016/j.peptides.2006.01.017
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access

Data sourced from Thomson Reuters' Web of Knowledge

Request changes or add full text files to a record

Repository staff actions (login required)

View Item View Item
twitter

Email us: wrap@warwick.ac.uk
Contact Details
About Us