Structurally biased random peptide libraries based on...

Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving nucleic acid

Reexamination Certificate

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C435S320100, C435S325000, C435S252300

Reexamination Certificate

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06936421

ABSTRACT:
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.

REFERENCES:
patent: 5223409 (1993-06-01), Ladner et al.
patent: 5824483 (1998-10-01), Houston et al.
patent: 6025485 (2000-02-01), Kamb et al.
patent: 6180343 (2001-01-01), Anderson et al.
patent: 6232107 (2001-05-01), Bryan et al.
patent: 6548249 (2003-04-01), Anderson et al.
patent: 6548632 (2003-04-01), Anderson et al.
patent: 6562617 (2003-05-01), Anderson et al.
patent: 6596485 (2003-07-01), Anderson et al.
patent: 2003/0224412 (2003-12-01), Anderson et al.
patent: WO 95/34664 (1995-12-01), None
patent: WO 97/11094 (1997-03-01), None
patent: WO 97/45538 (1997-12-01), None
patent: WO 98/36097 (1998-08-01), None
patent: WO 98/39483 (1998-09-01), None
patent: WO 99/24617 (1999-05-01), None
patent: WO 99/49019 (1999-09-01), None
Abedi et al., (1998) “Green fluorescent protein as a scaffold for intracellular presentation of peptides,”Nucl. Acids Res., 26:623-630.
Borjigin et al., “Insertional Mutagenesis as a Probe of Rhodopsin's Topography, Stability, and Activity,” Journal of Biological Chemistry, 269(20):14715-14722 (1994).
Cepko in Unit 9.9, pp. 9.9.1-9.9.16 in Current Protocols in Molecular Biology, Ausubel et al. Eds. John Wiley & Sons, 1996.
Dol et al., “Screening of conformationally constrained random polypeptide libraries displayed on a protein scaffold,” CMLS Cellular and Molecular Life Sciences, 54:394-404 (1998).
Hellinga et al., “Construction of New Ligand Binding Sites in Proteins of Known Structure,” J. Mol. Biol. 222:787-803 (1991).
Ladner et al., “Constrained peptides as binding entities,” TIBTECH, 13:426-430 (1995).
McConnell et al. “Tendamistat as a scaffold for conformationally constrained phage peptide libraries” J Mol Biol 250:460-470 (1995).
Ward et al. (1979) An energy transfer protein in coelenterate bioluminescence, J. Biol. Chem. 254(3):781-788.
Adachi, et al., “Site-Directed Mutants, at Position 166, of RTEM-1 beta-lactamase that Form a Stable acyl-enzyme Intermediate with Penicillin,” J. Biol. Chem., 266(5): 3186-3191 (Feb. 15, 1991).
Betz, et al., “Controlling Topology and Native-Like Behavior of de Novo-Designed Peptides: Design and Characterization of Antiparallel Four-Stranded Coiled Coils,” Biochemistry, 35(21):6955-6962 (May 1986).
Bouthors, et al., “Role of Residues 104, 164, 166, 238 and 240 in the Substrate Profile of PER-1 bata-lactamase Hydrolysing Third-Generation Cephalosporins,” Biochem J., 33Q(Pt. 3): 1443-1449 (Mar. 15, 1998).
Chalfie “Green fluorescent protein,” (1995) Photochemistry and Photobioligy, 62(4):651-656.
de Prat Gay, et al., “Generation of a Family of Protein Fragments fro Structure-Folding Studies. 1. Folding Complementation of Two Fragments of Chymotrypsin Inhibitor-2 formed by Cleavage at its unique Methionine Residue,” Biochemistry, 33(25): 7957-7963 (Jun. 28, 1994).
Doig, et al., “N- and C-Capping Preferences for all 20 Amino Acids in Alpha-Helical Peptides,” Protein Sci., 4(7): 1325-1336 (Jul. 1995).
Doig, et al., “Structures of N-Termini of Helices in Proteins,” Protein Sci, 6(1):147-155.
Graddis, et al., “Controlled Formation of Model Homo- and Heterodimer Coiled Coil Polypeptides,” Biochemistry, 32(47):12664-12671 (Nov. 1993).
Huang, et al., “A Natural Polymorphism in beta-lactamase is a Global Suppressor,” Proc. Natl. Acad. Sci. USA., 94(16): 8801-8806 (Aug. 5, 1997).
Jackson, et al., “Folding of Chymotrypsin Inhibitor 2. 1. Evidence for a Two-State Transition,” Biochemistry, 30(43): 10428-10435 (Oct. 29, 1991).
Jelsch, et al., “Crystal Structure ofEscherichia coliTEM1 beta-lactamase at 1.8 A Resolution,” Proteins, 16(4): 364-383 (Aug. 1993).
Knox, et al., “A Catalytically-Impaired Class A beta-lactamase: 2 A Crystal Structure and Kinetics of the Bacillus Licheniformis E166A Mutant,” Protein Eng., 6(1): 11-18 (Jan. 1993).
Legendre, et al., “Engineering of Regulatable Enzyme for Homogeneous Immunoassays,” Nat. Biotechnol., 17(1): 67-72 (Jan. 1999).
Longstaff, et al., “Recombinant Chymotrypsin Inhibitor 2: Expression, Kinetic Analysis of Inhibition with alpha-Chymotrypsin and wild-type and Mutant Subtilisin BPN', and Protein Engineering to Investigate inhibitory Specificity and Mechanism,” Biochemistry, 29(31): 7339-73347 (Aug. 7, 1990).
Lyu, et al., “Side Chain Contribution to the Stability of Alpha-Helical Structure in Peptides,” Science, 250(49811:669-673 (Nov. 1990).
Marshall, et al., “Evaluation of S1 Chromogenic Cephalosporin Beta-Lactamase Disk Assay Tested Against Gram-Positive Anaerobes, Coagulase-negativeStaphylococci, Prevotellaspp. andEnterococcusspp.,” Diagn. Microbiol. Infect. Dis., 22(4):353-355 (Aug. 1995).
McPhalen, et al., “Crustal and Molecular Structure of the Serine Proteinase Inhibitor Cl-2 from Barley Seeds,” Biochemistry, 26(1): 261-269 (Jan. 13, 1987).
Monera, et al., “Comparison of Antiparallel and Parallel Two-Stranded Alpha-Helical Coiled-Coils. Design, Synthesis, and Characterization,” J. Biol. Chem., 268(26):19218-19227 (Sep. 15, 1993).
Norman et al., “Genetic Selection of Peptide Inhibitors of Biological Activity,” Science, 285(5427):591-595 (Jul. 23, 1999).

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