Cell-permeable fluorescent proteins

Details Cell-permeable fluorescent proteins Cell-permeable fluorescent proteins

2011-07-05

2011-07-05

Kam, Chih-Min (Department: 1656)

Chemistry: natural resins or derivatives; peptides or proteins;

Proteins, i.e., more than 100 amino acid residues

C435S069100, C435S069700, C536S023500

Reexamination Certificate

active

07973132

ABSTRACT:
This invention relates to methods and compositions for designing novel fluorescent proteins, preferably to a green fluorescent proteins (GFP). The engineered GFPs are modified by substituting negatively charged amino acids with positively charged amino acids on the exterior of the protein making the protein cell permeable. The ability of the engineered fluorescent proteins to permeate cells obviates the need for transfections, allowing these novel proteins to be used in numerous biological applications.

REFERENCES:
patent: 5777079 (1998-07-01), Tsien et al.
patent: 6469154 (2002-10-01), Tsien et al.
patent: 6638732 (2003-10-01), Evans
Cody, C.W., et al., “Chemical Structure of the Hexapeptide Chromophore of theAequoreaGreen-Fluorescent Protein,” Biochemistry 32:1212-1218 (1993).
Cormack, B.P., et al., “FACS-optimized mutants of the green fluorescent protein (GFP),” Gene 173:33-3 (1996).
Fuchs, S.M., et al., “Pathway for Polyarginine Entry into Mammalian Cells,” Biochemistry 43:2438-2444 (2004).
Fuchs, S.M., et al, “Visions & Reflections, Internalization of cationic peptides: the road less (or more?) traveled,” Cell. Mol. Life Sci. 63:1819-1822 (2006).
Fuchs, S.M., et al., “Polyarginine as a multifunctional fusion tag,” Protein Science 14:1538-1544 (2005).
Hanson, G.T., et al., “Green Fluorescent Protein Variants as Ratiometric Dual Emission pH Sensors. 1. Structural . . . ” Biochemistry 41:15477-15488 (2002).
Hanson, G.T., et al., “Investigating Mitrochondrial Redox Potential with Redox-sensitive Green Fluorescent . . . ,” The Journal of Biological Chemistry 279:13044-13053 (2004).
Hoffman, R.M., “The Multiple Uses of Fluorescent Proteins to Visualize Cancer in vivo,” Nature 5:796-806 (2005).
Marafino, B.J., Jr., et al., “Commercial Development Considerations for Biotechnology-Derive Therapeutics,” Cardiovascular Toxicology 03:5-12 (2003).
Pace, C.N., et al., “Charge-charge interactions influence the denatured state ensemble and contribute to protein stability,” Protein science 9:1395-1398 (2000).
Richard. J.P., et al., “Cellular Uptake of Unconjugated TAT Peptide Involves Clathrin-dependent Endocytosis and Heparan . . . ,” The Journal of Biological Chemistry 280:15300-15306 (2005).
Rosenow, M.A., et al., “The Crystal Structure of the Y66L Variant of Green Fluorescent Protein Supports a Cyclization-Oxidation-Dehydration Mechanism . . . ,” Biochemistry 43:4464-4472 (2004).
Stepanenko, O.V., et al., “Comparative Studies on the Structure and Stability of Fluorescent Proteins EGFP, zFP506, mRFP1, “dimer2”, and DsRed1.” Biochemistry 43:14913-14923 (2004).
Waldo, G.S., et al., “Rapid protein-folding assay using green fluorescent protein,” Nature Biotechnology 17:691-695 (1999).
Ward, T.H., “The Uses of Green Fluorescent Protein in Mammalian Cells,” Green Fluorescent Protein: Properties, Applications, and Protocols. Second Edition 305-337 (2006).
Zacharias, D.A., “Molecular Biology and Mutation of Green Fluorescent Protein,” Green Fluorescent Protein: Properties, Applications, and Protocols, Second Edition 83-120 (2006).

Affiliated with

Also associated with

Rating

Cell-permeable fluorescent proteins does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Cell-permeable fluorescent proteins, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Cell-permeable fluorescent proteins will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-2737480