From peptides to drugs via phage display

In the past ten years, there has been a flurry of research generating and screening combinatorial peptide libraries. Molecular biologists have favored phage display as a means of generating millions to billions of different peptides for the purposes of mapping protein–protein interactions of antibod...

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Published in:	Drug discovery today Vol. 3; no. 8; pp. 370 - 378
Main Authors:	Kay, Brian K., Kurakin, Alexei V., Hyde-DeRuyscher, Robin
Format:	Journal Article
Language:	English
Published:	Oxford Elsevier Ltd 01-08-1998 Elsevier Science
Subjects:	Biological and medical sciences combinatorial chemistry General pharmacology high-throughput screening Medical sciences peptidomimetics Pharmaceutical technology. Pharmaceutical industry Pharmacology. Drug treatments protein–protein interaction target validation protein–protein interaction peptidomimetics combinatorial chemistry target validation high-throughput screening Virus Drug Pharmaceutical technology Targeting Peptides Peptidomimetic compound Review Molecular biology Research and development Phage
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Abstract	In the past ten years, there has been a flurry of research generating and screening combinatorial peptide libraries. Molecular biologists have favored phage display as a means of generating millions to billions of different peptides for the purposes of mapping protein–protein interactions of antibodies, cell surface receptors and intracellular proteins. This article summarizes recent work on identifying peptide ligands via phage display and several methods by which they serve to promote drug discovery: design of peptidomimetics, biological validation of targets, and the establishment of high-throughput screens of chemical compound libraries. These methods provide powerful aids in the search for lead compounds of previously `unscreenable' targets and for new targets discovered in genomics efforts.
AbstractList	In the past ten years, there has been a flurry of research generating and screening combinatorial peptide libraries. Molecular biologists have favored phage display as a means of generating millions to billions of different peptides for the purposes of mapping protein-protein interactions of antibodies, cell surface receptors and intracellular proteins. This article summarizes recent work on identifying peptide ligands via phage display and several methods by which they serve to promote drug discovery: design of peptidomimetics, biological validation of targets, and the establishment of high-throughput screens of chemical compound libraries. These methods provide powerful aids in the search for lead compounds of previously 'unscreenable' targets and for new targets discovered in genomics efforts.
Author	Hyde-DeRuyscher, Robin Kay, Brian K. Kurakin, Alexei V.
Author_xml	– sequence: 1 givenname: Brian K. surname: Kay fullname: Kay, Brian K. organization: Department of Pharmacology, University of Wisconsin-Madison, 1300 University Avenue, Madison, WI 53706-1532, USA – sequence: 2 givenname: Alexei V. surname: Kurakin fullname: Kurakin, Alexei V. organization: Department of Pharmacology, University of Wisconsin-Madison, 1300 University Avenue, Madison, WI 53706-1532, USA – sequence: 3 givenname: Robin surname: Hyde-DeRuyscher fullname: Hyde-DeRuyscher, Robin organization: Novalon Pharmaceutical Corp., 4222 Emperor Blvd, Suite 560, Durham, NC 27703-8466, USA
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Snippet	In the past ten years, there has been a flurry of research generating and screening combinatorial peptide libraries. Molecular biologists have favored phage...
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SubjectTerms	Biological and medical sciences combinatorial chemistry General pharmacology high-throughput screening Medical sciences peptidomimetics Pharmaceutical technology. Pharmaceutical industry Pharmacology. Drug treatments protein–protein interaction target validation
Title	From peptides to drugs via phage display
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