Source:http://linkedlifedata.com/resource/pubmed/id/16517013
Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
7
|
| pubmed:dateCreated |
2006-6-19
|
| pubmed:abstractText |
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 UDP-N-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 microM 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.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jul
|
| pubmed:issn |
0196-9781
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
27
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1693-700
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:16517013-Amino Acid Motifs,
pubmed-meshheading:16517013-Amino Acid Sequence,
pubmed-meshheading:16517013-Binding Sites,
pubmed-meshheading:16517013-Computational Biology,
pubmed-meshheading:16517013-Dose-Response Relationship, Drug,
pubmed-meshheading:16517013-Inhibitory Concentration 50,
pubmed-meshheading:16517013-Ligases,
pubmed-meshheading:16517013-Models, Chemical,
pubmed-meshheading:16517013-Molecular Sequence Data,
pubmed-meshheading:16517013-Peptide Library,
pubmed-meshheading:16517013-Peptides,
pubmed-meshheading:16517013-Protein Binding,
pubmed-meshheading:16517013-Protein Conformation,
pubmed-meshheading:16517013-Pseudomonas aeruginosa,
pubmed-meshheading:16517013-Sequence Analysis, DNA,
pubmed-meshheading:16517013-Sequence Homology, Amino Acid,
pubmed-meshheading:16517013-Spectrophotometry
|
| pubmed:year |
2006
|
| pubmed:articleTitle |
Selection of peptide inhibitors against the Pseudomonas aeruginosa MurD cell wall enzyme.
|
| pubmed:affiliation |
CREFSIP, Département de Biologie Médicale, Faculté de Médecine, Université Laval, Sainte-Foy, Québec, Canada G1K 7P4. cparadis@rsvs.ulval.ca
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|