Abstract
A highly potent CXCR4 antagonist 2 [cyclo (-D-Tyr1-Arg2-Arg3-Nal4-Gly5-)] has previously been identified by screening cyclic pentapeptide libraries that were designed based on pharmacophore residues of a 14-residue peptidic CXCR4 antagonist 1. In the present study, D-Tyr and Arg in peptide 2 were replaced by a bicyclic aromatic amino acid and a cationic amino acid, respectively, and their binding activity for CXCR4 was evaluated for identification of the novel pharmacophore.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Animals
-
Cattle
-
Cell Line
-
Drug Discovery*
-
HIV-1 / drug effects
-
Humans
-
Oligopeptides / chemical synthesis
-
Oligopeptides / chemistry*
-
Oligopeptides / pharmacology*
-
Oligopeptides / toxicity
-
Peptides, Cyclic / chemical synthesis
-
Peptides, Cyclic / chemistry*
-
Peptides, Cyclic / pharmacology*
-
Peptides, Cyclic / toxicity
-
Receptors, CXCR4 / antagonists & inhibitors*
-
Structure-Activity Relationship
-
Tyrosine / chemistry
Substances
-
Oligopeptides
-
Peptides, Cyclic
-
Receptors, CXCR4
-
Tyrosine