Abstract: Novel polypeptides having functional domains of interest are described, along with DNA sequences that encode the same. A method of identifying these polypeptides by means of a sequence-independent (that is, independent of the primary sequence of the polypeptide sought), recognition unit-based functional screen is also disclosed. Various applications of the method and of the polypeptides identified are described, including their use in assay kits for drug discovery, modification, and refinement.
Type:
Grant
Filed:
June 13, 2001
Date of Patent:
March 23, 2004
Assignees:
University of North Carolina at Chapel Hill, Cytogen Corp.
Inventors:
Andrew B. Sparks, Noah Hoffman, Brian K. Kay, Dana M. Fowlkes, Stephen J. McConnell
Abstract: Novel polypeptides having functional domains of interest are described, along with DNA sequences that encode the same. A method of identifying these polypeptides by means of a sequence-independent (that is, independent of the primary sequence of the polypeptide sought), recognition unit-based functional screen is also disclosed. Various applications of the method and of the polypeptides identified are described, including their use in assay kits for drug discovery, modification, and refinement.
Type:
Grant
Filed:
April 3, 1996
Date of Patent:
October 30, 2001
Assignees:
University of North Carolina at Chapel Hill, Cytogen Corp.
Inventors:
Andrew B. Sparks, Noah Hoffman, Brian K. Kay, Dana M. Fowlkes, Stephen J. McConnell
Abstract: Peptides having general and specific binding affinities for the Src homology region 3 (SH3) domains of proteins are disclosed in the present invention. In particular, SH3 binding peptides have been isolated from phage-displayed random peptide libraries which had been screened for isolates that bind to bacterial fusion proteins having an SH3 domain and glutathione S-transferase (GST). Preferred peptides are disclosed which comprise a core 7-mer sequence (preferably, a consensus motif) and two or more, preferably at least six, additional amino acid residues flanking the core sequence, for a total length of 9, preferably at least 13, amino acid residues and no more than about 45 amino acid residues. Such peptides manifest preferential binding affinities for certain SH3 domains. The preferred peptides exhibit specific binding affinities for the Src-family of proteins. In vitro and in vivo results are presented which demonstrate the biochemical activity of such peptides.
Type:
Grant
Filed:
February 16, 1996
Date of Patent:
February 6, 2001
Assignees:
University of North Carolina at Chapel Hill, Cytogen Corp.
Inventors:
Andrew B. Sparks, Brian K. Kay, Judith M. Thorn, Lawrence A. Quilliam, Channing J. Der, Dana M. Fowlkes, James E. Rider
Abstract: Novel polypeptides having WW domains of interest are described, along with DNA sequences that encode the same. A method of identifying these polypeptides by means of a sequence-independent (that is, independent of the primary sequence of the polypeptide sought), recognition unit-based functional screen is also disclosed. Various applications of the method and of the polypeptides identified are described, including their use in assay kits for drug discovery, modification, and refinement.
Type:
Grant
Filed:
April 3, 1996
Date of Patent:
January 4, 2000
Assignees:
University of North Carolina at Chapel Hill, Cytogen Corp.
Inventors:
Gregorio Pirozzi, Brian K. Kay, Dana M. Fowlkes