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Selection of peptides with antibody-like properties

a technology of antibody-like properties and peptides, applied in the fields of protein chemistry, biochemistry, organic chemistry and molecular biology, can solve the problems of unfavorable high-throughput proteomic applications, and tedious and imperfect processes, and achieve the effect of facilitating binding of said complexes

Inactive Publication Date: 2006-12-07
KODADEK THOMAS
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

This would obviate the need to create epitope-tagged versions of the native proteins for the purpose of immunoaffinity chromatography, a tedious and imperfect process that is not well-suited for high-throughput proteomic applications.
As stated above, a priori, it was not clear how feasible this endeavor would be.
This kind of shielding is not possible for complexes between small peptides.
Additionally, most peptides do not adopt stable secondary or tertiary structures, leading to the expectation that the entropic cost of forming a complex between small peptides would be much higher than binding of a peptide to a structurally well-defined protein.
These approaches failed completely.

Method used

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  • Selection of peptides with antibody-like properties
  • Selection of peptides with antibody-like properties
  • Selection of peptides with antibody-like properties

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Embodiment Construction

[0036] As discussed, an important goal in chemical biology is to be able to obtain specific ligands for any biomolecule of interest. Impressive advances have been made in isolating molecules, many of which are antibodies or antibody-derived, that bind proteins and nucleic acid targets with well-defined macromolecular structures. However, the identification of sequence-specific, peptide-binding ligands has been more difficult. In addition, even antibodies have major drawbacks: they are tedious and expensive to generate, difficult to produce in large quantities, are relatively fragile molecules unsuitable for certain field applications, and often bind so tightly that they or their target proteins are damaged upon attempted extraction. Natural peptide-binding proteins or protein domains have been mutagenized to derive species with novel binding specificities (Schneider et al., 1999), but like antibodies, these are globular macromolecules. Thus, though the development of synthetic recep...

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Abstract

The present invention provides a highly sensitive screening assay for the identification of peptide binding partners to virtually any peptide or polypeptide ligand. Utilizing an expression-repression readout system, the inventors have screened libraries of peptides and identified relatively small peptide molecules that bind to the provided target.

Description

[0001] The present application claims priority to U.S. Provisional Patent Application Ser. No. 60 / 182,060, filed Feb. 11, 2000, the entire text of which is specifically incorporated by reference herein without disclaimer.BACKGROUND OF THE INVENTION [0002] A. Field of the Invention [0003] The present invention relates generally to the fields of protein chemistry, biochemistry, organic chemistry and molecular biology. More particularly, it concerns a novel screen for identifying peptides having target binding affinity. [0004] B. Description of Related Art [0005] With the end of the human genome project in sight, the next great challenge in human biology will be to deduce the function of the thousands of new gene products identified by the sequencing effort. Perhaps the most direct way to take advantage of knowing the sequences of these proteins would be to design compounds capable of binding specific epitopes in a factor of interest. These binding agents could then be used for a varie...

Claims

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Application Information

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Patent Type & Authority Applications(United States)
IPC IPC(8): C40B30/06C40B40/10C40B50/06C12P21/08C12Q1/68C40B30/04G01N33/68
CPCC12Q1/6897G01N33/6845G01N33/6842C40B30/04
Inventor KODADEK, THOMAS
Owner KODADEK THOMAS
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