Linked Life Data

20422669

Source:http://linkedlifedata.com/resource/pubmed/id/20422669

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2010-5-17
pubmed:abstractText
Various synthetic cyclopeptides bind different cellular proteins with high affinity and specificity. In this study, we designed a new series of cyclic tetrapeptides containing the RGD sequence, a ligand for the alpha(v)beta(3) integrin receptor, in which the ring closure was performed through a urea bond between the alpha-amino group of the peptide and either the alpha- or the epsilon-amino group of an additional lysine. Interestingly, we showed that the urea-closed peptide had a higher affinity for alpha(v)beta(3) receptors than a reference pentacyclopeptide. Moreover, the synthetic strategy allows coupling of the resulting cyclic tetrapeptide through the carboxylic acid moiety of its lysine residue to fluorescent molecules or drugs. In addition, this strategy could be easily adapted for the cyclization of any other peptides.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1439-7633
pubmed:author
pubmed:issnType
Electronic
pubmed:day
17
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1083-92
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Cyclization of peptides through a urea bond: application to the Arg-Gly-Asp tripeptide.
pubmed:affiliation
Institut de Recherche en Cancérologie de Montpellier, Université Montpellier1, Montpellier, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't