NDLI: High-affinity urokinase receptor antagonists identified with bacteriophage peptide display.

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High-affinity urokinase receptor antagonists identified with bacteriophage peptide display.

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High-affinity urokinase receptor antagonists identified with bacteriophage peptide display.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Doyle, M. V. Rosenberg, S. Goodson, R. J. Kaufman, S. E.
Description	Author Affiliation: Goodson RJ ( Chiron Corporation, Emeryville, CA 94608.);
Abstract	Affinity selection of a 15-mer random peptide library displayed on bacteriophage M13 has been used to identify potent ligands for the human urokinase receptor, a key mediator of tumor cell invasion. A family of receptor binding bacteriophage ligands was obtained by sequentially and alternately selecting the peptide library on COS-7 monkey kidney cells and baculovirus-infected Sf9 insect cells overexpressing the human urokinase receptor. Nineteen peptides encoded by the random DNA regions of the selected bacteriophage were synthesized and tested in a urokinase receptor binding assay, where they competed with the labeled N-terminal fragment of urokinase with IC50 values ranging from 10 nM to 10 microM. All of the isolated peptides were linear and showed two relatively short conserved subsequences: LWXXAr (Ar = Y, W, F, or H) and XFXXYLW, neither of which is found in urokinase or its receptor. Competition experiments demonstrated that the most potent peptide, clone 20, prevented binding of bacteriophage displaying the urokinase receptor binding sequence (urokinase residues 13-32). In addition, this peptide blocked other apparently unrelated receptor binding bacteriophage, suggesting overlapping receptor interaction sites for all of these sequences. These results provide a demonstration of bacteriophage display identifying peptide ligands for a receptor expressed on cells and yield leads for the development of urokinase receptor antagonists.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	15
Volume Number	91
Language	English
Publisher	National Academy of Sciences
Publisher Date	1994-08-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bacteriophage M13 Metabolism Receptors, Cell Surface Antagonists & Inhibitors Urokinase-Type Plasminogen Activator Viral Proteins Amino Acid Sequence Animals Binding, Competitive Cell Line DNA Molecular Sequence Data Peptides Receptors, Urokinase Plasminogen Activator Recombinant Proteins Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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