Synthesis and erythropoietin receptor binding affinities of N,N-disubstituted amino acids

N,N-Dicinnamyl, N-benzyl- N-cinnamyl, and N,N-dibenzyl amino acids were prepared and evaluated in an EPO binding assay. Several derivatives of aspartic acid, glutamic acid, and lysine exhibited moderate (10–50 μM) affinity for EBP; ‘dimerization’ of the most potent analogues by coupling with linear...

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Published inBioorganic & medicinal chemistry letters Vol. 10; no. 17; pp. 1995 - 1999
Main Authors Connolly, Peter J, Wetter, Steven K, Murray, William V, Johnson, Dana L, McMahon, Frank J, Farrell, Francis X, Tullai, Jennifer, Jolliffe, Linda K
Format Journal Article
LanguageEnglish
Published Oxford Elsevier Ltd 04.09.2000
Elsevier
Subjects
Amino Acids - chemical synthesis
Amino Acids - metabolism
Biological and medical sciences
Blood. Blood coagulation. Reticuloendothelial system
Dimerization
Medical sciences
Pharmacology. Drug treatments
Receptors, Erythropoietin - metabolism
Protecting group
Spacer arm
Erythropoietin
Aminoamide
In vitro
Biological fixation
Growth factor receptor
Structure activity relation
Benzylic compound
Glycopeptide
Dicarboxylic acid
Dimer
Diether
Chemical synthesis
Biological receptor
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Summary:N,N-Dicinnamyl, N-benzyl- N-cinnamyl, and N,N-dibenzyl amino acids were prepared and evaluated in an EPO binding assay. Several derivatives of aspartic acid, glutamic acid, and lysine exhibited moderate (10–50 μM) affinity for EBP; ‘dimerization’ of the most potent analogues by coupling with linear diamines led to EPO competitors having 1–2 μM binding affinities.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0960-894X
1464-3405
DOI:10.1016/S0960-894X(00)00399-1