Linked Life Data

15177470

Source:http://linkedlifedata.com/resource/pubmed/id/15177470

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
2004-6-4
pubmed:abstractText
(S)-4-(Carboxamido)phenylalanine (Cpa) is examined as a bioisosteric replacement for the terminal tyrosine (Tyr) residue in a variety of known peptide ligands for the mu, delta and kappa opioid receptors. The Cpa-containing peptides, assayed against cloned human opioid receptors, display comparable binding affinity (Ki), and agonist potency (EC50) to the parent ligands at the three receptors. Cpa analogs of delta selective peptides show an increase in delta selectivity relative to the mu receptor. Cpa is the first example of an amino acid that acts as a surrogate for Tyr in opioid peptide ligands, challenging the long-standing belief that a phenolic residue is required for high affinity binding.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0960-894X
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3545-8
pubmed:dateRevised
2005-2-3
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
(4-Carboxamido)phenylalanine is a surrogate for tyrosine in opioid receptor peptide ligands.
pubmed:affiliation
Department of Chemistry, Adolor Corporation, 700 Pennsylvania Drive, Exton, PA 19341, USA. rdolle@adolor.com
pubmed:publicationType
Journal Article