Brian K. Kay - Chapel Hill NC Andrew B. Sparks - Carrboro NC Judith M. Thorn - Carrboro NC Lawrence A. Quilliam - Chapel Hill NC Channing J. Der - Chapel Hill NC
Assignee:
The University of North Carolina at Chapel Hill - Chapel Hill NC
Peptides having general and specific binding affinities for the Src homology region (SH3) domains of proteins are disclosed in the present invention. In particular, SH3 binding peptides have been isolated from three phage-displayed random peptide libraries which had been screened for isolates that bind to bacterial fusion proteins of SH3 domains and glutathione S-transferase (GST). Preferred peptides are disclosed having 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.
Brian K Kay - Chapel Hill NC Dana M. Fowlkes - Chapel Hill NC Nils B. Adey - Carrboro NC Andrew B. Sparks - Carrboro NC
Assignee:
The University of North Carolina at Chapel Hill - Chapel Hill NC
International Classification:
C12N 1509 C12N 510 C12N 1562
US Classification:
4353201
Abstract:
A novel method for producing novel and/or improved heterofunctional binding fusion proteins termed Totally Synthetic Affinity Reagents (TSARs) is disclosed. TSARs are concatenated heterofunctional proteins, polypeptides or peptides comprising at least two functional regions: a binding domain with affinity for a ligand and a second effector peptide portion that is chemically or biologically active. In one embodiment, the heterofunctional proteins, polypeptides or peptides further comprise a linker peptide portion between the binding domain and the second active peptide portion. The linker peptide can be either susceptible or not susceptible to cleavage by enzymatic or chemical means. Novel and/or improved heterofunctional binding reagents as well as methods for using the reagents for a variety of in vitro and in vivo applications are also disclosed.
Scr Sh3 Binding Peptides And Methods Of Isolating And Using Same
Brian K. Kay - Chapel Hill NC Andrew B. Sparks - Carrboro NC Judith M. Thorn - Carrboro NC Lawrence A. Quilliam - Chapel Hill NC Channing J. Der - Chapel Hill NC
Assignee:
The University of North Carolina at Chapel Hill - Chapel Hill NC
International Classification:
A61K 3810 C07K 708
US Classification:
514 14
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 three phage-displayed random peptide libraries which had been screened for isolates that bind to bacterial fusion proteins of SH3 domains and glutathione S-transferase (GST). Preferred peptides are disclosed having 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.
Brian K Kay - Chapel Hill NC Dana M. Fowlkes - Chapel Hill NC Nils B. Adey - Carrboro NC Andrew B. Sparks - Carrboro NC
Assignee:
University of North Carolina at Chapel Hill - Chapel Hill NC
International Classification:
C12N 1509 C12N 1562
US Classification:
435 691
Abstract:
A novel method for producing novel and/or improved heterofunctional binding fusion proteins termed Totally Synthetic Affinity Reagents (TSARs) is disclosed. TSARs are concatenated heterofunctional proteins, polypeptides or peptides comprising at least two functional regions: a binding domain with affinity for a ligand and a second effector peptide portion that is chemically or biologically active. In one embodiment, the heterofunctional proteins, polypeptides or peptides further comprise a linker peptide portion between the binding domain and the second active peptide portion. The linker peptide can be either susceptible or not susceptible to cleavage by enzymatic or chemical means. Novel and/or improved heterofunctional binding reagents as well as methods for using the reagents for a variety of in vitro and in vivo applications are also disclosed.
Grb2 Sh3 Binding Peptides And Methods Of Isolating And Using Same
Andrew B. Sparks - Carrboro NC Brian K. Kay - Chapel Hill NC Judith M. Thorn - Carrboro NC Lawrence A. Quilliam - Indianapolis IN Channing J. Der - Chapel Hill NC Dana M. Fowlkes - Chapel Hill NC James E. Rider - Carrboro NC
Assignee:
University of North Carolina at Chapel Hill - Chapel Hill NC Cytogen Corp. - Princeton NJ
International Classification:
A61K 3810 C07K 708
US Classification:
514 13
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.
Polypeptides Having A Functional Domain Of Interest And Methods Of Identifying And Using Same
Andrew B. Sparks - Carrboro NC Noah Hoffman - Greensboro NC Brian K. Kay - Chapel Hill NC Dana M. Fowlkes - Chapel Hill NC Stephen J. McConnell - San Diego CA
Assignee:
University of North Carolina at Chapel Hill - Chapel Hill NC Cytogen Corp. - Princeton NJ
International Classification:
C12Q 168 G01N 3353 A61K 3800 C12N 700
US Classification:
435 6
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.
Blair Elementary School Fairchild Afb WA 1990-1992, Lakenheath American Elementary School Lakenheath CT 1992-1996, Nathan Twining Middle School Grand Forks ND 1996-1998, McNabb Middle School Mt. Sterling KY 1998-1999
Colin Marang, Brealyn Brashier, Shanesta Witte, Taylor Rogers, Logan Branch, Jared Abbott, Emily Rush, Raymond Young, Ronald Stiehler, Jose Sandoval, Patrick Folmar
attorneys Andrew Sparks and Paul McCaffrey claim that from 2004 to 2008, numerous patients suffered serious injuries because nursing home personnel didn't follow physicians' orders, didn't properly treat bed sores, didn't update resident care plans, and didn't monitor blood-sugar levels of diabetic