Linked Life Data

7700843

Source:http://linkedlifedata.com/resource/pubmed/id/7700843

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1995-5-1
pubmed:abstractText
The effect of structural changes in the N-terminal amino acid of AIV, with respect to AT4 receptor binding, was examined by competition with [125I]AIV in bovine adrenal membranes. Analogues with modifications of the first residue alpha-amino group possessed lower affinities than the primary amine-containing parent compound. Peptides with a residue 1 alpha-carbon in the D conformation exhibited poor affinity for the AT4 receptor. Modifications of the residue 1 R-group demonstrate that a straight chain aliphatic moiety containing four carbons is optimal for receptor-ligand binding, as evidenced by the extremely high affinity of [Nle1]AIV (Ki = 3.59 +/- 0.51 pM). Replacement of the 1-2 peptide bond of AIV with the methylene bond isostere psi (CH2-NH), increased the Ki approximately fivefold, indicating that the peptide bond may be replaced while maintaining relatively high-affinity receptor binding.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0196-9781
pubmed:author
pubmed:issnType
Print
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1399-406
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
AT4 receptor structure-binding relationship: N-terminal-modified angiotensin IV analogues.
pubmed:affiliation
Department of Veterinary and Comparative Anatomy, Pharmacology, and Physiology, Washington State University, Pullman 99164-6520.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't