Rigel Pharmaceuticals, Incorporated

The University of Texas System

Other

Massachusetts Institute of Technology

Becton Dickinson and Company Limited

Beau R Peelle

David C Anderson

Jakob Maria Bogenberger

Angela M Belcher

Ki Tae Nam

Karl Dane Wittrup

Eric Krauland

One-dimensional ring structures from M13 viruses were constructed by two genetic modifications encoding binding peptides and synthesis of a heterobifunctional linker molecule. The bifunctional viruses displayed an anti-streptavidin peptide and hexahistidine (SEQ ID NO:4) peptide at opposite ends of the virus as pIII and pIX fusions. Stoichiometric addition of the streptavidin-NiNTA linker molecule led to the reversible formation of virus-based nanorings with circumferences corresponding to lengths of the packagable DNAs. These virus-based ring structures can be further engineered to nucleate inorganic materials and form metallic, magnetic, or semiconductor nanorings using trifunctionalized viruses.

Multifunctional biomaterials as scaffolds for electronic, optical, magnetic, semiconducting, and biotechnological applications

Eukaryotic cell display libraries for use in panning processes comprising expressed biomolecules for specific and selective binding and enrichment to solid material surfaces including, for example, metal, magnetic, and semiconducting surfaces. Display can be regulated. Peptide and protein display on yeast cells are preferred. Solid materials can be fabricated in the presence of cell display libraries which have been subjected to panning against the solid materials. Nanoparticles can be grown in the presence of the biomolecules from reactive precursors. The nanoparticles can show quantum confinement effects. Self-healing films can be prepared.

Cell display libraries

One-dimensional ring structures from M13 viruses were constructed by two genetic modifications encoding binding peptides and synthesis of a heterobifunctional linker molecule. The bifunctional viruses displayed an anti-streptavidin peptide and hexahistidine (SEQ ID NO:4) peptide at opposite ends of the virus as pIII and pIX fusions. Stoichiometric addition of the streptavidin-NiNTA linker molecule led to the reversible formation of virus-based nanorings with circumferences corresponding to lengths of the packageable DNAs. These virus-based ring structures can be further engineered to nucleate inorganic materials and form metallic, magnetic, or semiconductor nanorings using trifunctionalized viruses.

The invention relates to methods and compositions utilizinggreen fluorescent proteins (rGFP), andgreen fluorescent proteins (pGFP). In particular, the invention relates to the use ofGFP orGFP proteins as reporters for cell assays, particularly intracellular assays, including methods of screening libraries using rGFP or pGFP.

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One-dimensional ring structures form M13 viruses were constructed by two genetic modifications encoding binding peptides and synthesis of a heterobifunctional linker molecule. The bifunctional viruses displayed an anti-streptavidin peptide and hexahistidine (SEQ ID NO: 4) peptide at opposite ends of the virus as pIII and pIX fusions. Stoichiometic addition of the streptavidin-NiNTA linker molecule led to the reversible formation of virus-based nanorings with circumferences corresponding to lengths of the packagable DNAs. These virus-based ring structures can be further engineered to nucleate inorganic materials and form metallic, magnetic, or semiconductor nanorings using trifunctionalized viruses.

The invention relates to the use of scaffold proteins, particularly green fluorescent protein (GFP), in fusion constructs with random and defined peptides and peptide libraries, to increase the cellular expression levels, decrease the cellular catabolism, increase the conformational stability relative to linear peptides, and to increase the steady state concentrations of the library peptides and peptide library members expressed in cells for the purpose of detecting the presence of the peptides and screening peptide libraries. N-terminal, C-terminal, dual N- and C-terminal and one or more internal fusions are all contemplated. Novel fusions utilizing self-binding peptides to create a conformationally stabilized fusion domain are also contemplated.

Structurally biased random peptide libraries based on different scaffolds

The present invention relates to directed protein evolution in mammalian cells and improved mutants of Discosoma sp. red fluorescent proteins.

Discosoma red fluorescent proteins

Directed evolution of protein in mammalian cells

The invention relates to the use of scaffold proteins, particularly green fluorescent protein (GFP), in fusion constructs with random and defined peptides and peptide libraries, to increase the cellular expression levels, decrease the cellular catabolism, increase the conformational stability relative to linear peptides, and to increase the steady state concentrations of the random peptides and random peptide library members expressed in cells for the purpose of detecting the presence of the peptides and screening random peptide libraries. N-terminal, C-terminal, dual N- and C-terminal and one or more internal fusions are all contemplated. Novel fusions utilizing self-binding peptides to create a conformationally stabilized fusion domain are also contemplated.

Growing community of inventors

Cambridge, MA, United States of America

Beau R Peelle