Membrane scaffold proteins and embedded membrane proteins

Details Membrane scaffold proteins and embedded membrane proteins Membrane scaffold proteins and embedded membrane proteins

2006-05-23

2010-02-16

Li, Ruixiang (Department: 1646)

Drug, bio-affecting and body treating compositions

Preparations characterized by special physical form

Particulate form

C530S350000, C530S402000

Reexamination Certificate

active

07662410

ABSTRACT:
Membrane proteins are difficult to express in recombinant form, purify, and characterize, at least in part due to their hydrophobic or partially hydrophobic properties. Membrane scaffold proteins (MSP) assemble with target membrane or other hydrophobic or partially hydrophobic proteins or membrane fragments to form soluble nanoscale particles which preserve their native structure and function; they are improved over liposomes and detergent micelles. In the presence of phospholipid, MSPs form nanoscopic phospholipid bilayer disks, with the MSP stabilizing the particle at the perimeter of the bilayer domain. The particle bilayer structure allows manipulation of incorporated proteins in solution or on solid supports, including for use with such surface-sensitive techniques as scanning probe microscopy or surface plasmon resonance. The nanoscale particles facilitate pharmaceutical and biological research, structure/function correlation, structure determination, bioseparation, and drug discovery.

REFERENCES:
patent: 5652339 (1997-07-01), Lerch et al.
patent: 6172262 (2001-01-01), McQuade et al.
patent: 6248353 (2001-06-01), Singh
patent: 7048949 (2006-05-01), Sligar et al.
patent: 7083958 (2006-08-01), Sligar et al.
patent: 2005/0152984 (2005-07-01), Sligar et al.
patent: 2005/0182243 (2005-08-01), Sligar et al.
patent: 2006/0211092 (2006-09-01), Sligar et al.
patent: 0663407 (2007-07-01), None
patent: WO 93/17031 (1993-09-01), None
patent: WO 00/75187 (2000-12-01), None
patent: WO 01/02551 (2001-01-01), None
U.S. Appl. No. 11/870,217, Sligar et al.
Atkinson, D. and Small, D.M. (1986) “Recombinant Lipoproteins:Implications for Structure and Assembly of Native Lipoproteins”Ann. Rev. Biophys. Chem. 15:403-456.
Bakker, E.P. and Caplan, S.R. (1982), “Phospholipid Substitution of the Purple Membrane,” Methods in Enzymol. 88:26-30.
Bayburt, T.H. et al., (Dec. 2002) “Self-Assembly of Discoidal Phospholipid Bilayer Nanoparticles with Membrane Scaffold Proteins”;Nano Letters2:853-856.
Bayburt, T.H. et. al., (May 2002) “Single Molecule Height Measurements on Microsomal Cytochrome P450 in nanometer-Scale Phospholipid Bilayer Disks”;Proceedings of the National Academy of Sciences99:6725-6730.
Bayburt, T.H. et al. (Nov. 2003) “Self-Assembly of Single Integral Membrane Proteins into Soluble Nanoscale Phospholipid Bilayers”;Protein Science12:2476-2481.
Bayburt, T.H. et al. (1998) “Reconstitution and Imaging of a Membrane Protein in a Nanometer-Size Phospholipid bilayer”J. Struct. Biol. 123:37-44.
Bayburt, T.H. et al. (Jun. 2000) “Single Molecule Height Measurements on a Membrane Protein in Nanometer-Scale Phospholipid Bilayer Disks”Langmuir16(14):5993-5997.
Bayley, H. et al. (1982), “Delipidation, Renaturation, and Reconstitution of Bacberiorhodopsin,” Methods Enzymol. 88:74-81.
Bergeron et al. (1995) “Apolipoprotein A-I Confirmation in Reconstituted Discoidal Lipoproteins Varying in Phospholipid and Cholesterol Content,”J. Biol. Chem. 270:27429-27438.
Bergeron et al. (1997) “Characterization of Human Apolipoprotein A-I Expressed inEscherichia coli,” Biochim. Biophys. Acta. 1344:139-152.
Boguski, M.S. et al. (1986) “On computer-assisted analysis of biological sequences: proline punctuation, consensus sequences, and apolipoprotein repeats”J. of Lipid Research27:1011-1034.
Borhani, D.W. et al. (1997) “Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation”Proc. Natl. Acad. Sci. USA94:12291-12296.
Brouillette, C. et al., (2001), “Structural models of human apolipoprotein A-I: a critical analysis and reveiw,” Biochim. Biophys. Acta 1531:4-46.
Brouillette, C.G. et al. (1984) “Structural Studies of Apolipoprotein A-I/Phosphatidylcholine Recombinants by High-Field Proton NMR, Nondenaturing Gradient Gel Electrophoresis, and Electron Microscopy”Biochemistry23:359-367.
Bruhn et al. (1991) “An Approach to the Functional Analysis of Lecithin-Cholesterol Acryltransferase. Activation by Recominant Normal and Mutagenized Apolipoprotein AI,”Biological Chemistry Hoppe-Seyler372(3):225-234.
Burgess et al. (Nov. 2, 1999) “Deletion of the C-Terminal Domain of Apolipoprotein A-I Impairs Cell Surface Binding and Lipid Efflux in Macrophage,”Biochem. 38(44):14524-14533.
Carlson, J. W. et al. (Mar. 2000) “Nanopatterning Phospholipid Bilayers”Langmuir16(8):3927-3931.
Carlson, J.W. et al. (Sep. 1997) “Imaging and Manipulation of High-Density Lipoproteins”Biophys. J. 73:1184-1189.
Chen, J.S. et al., (2002)Insect Molecular Biology11:175-186.
Chromy et al. (2007) “Different Apolipoproteins Impact Nanolipoprotein Particle Formation,” J. Am. Chem. Soc. Oct. 27, 2007; [Epub ahead of Print], A-D, and supporting documents, S1-S8.
Civjan, N.R. et al., (2003) “Direct Solubilization of Heterologously Expressed Membrane Proteins by Incorporation into Nanoscale Lipid Bilayers”;BioTechniques35:556-563.
Dalton, M.B. and Swaney, J.B. (Sep. 15, 1993) “Structural and Functional Domains of Apolipoprotein A-I within High Density Lipoproteins”J. Biol. Chem. 268(26):19274-19283.
Dencher, N.A. and Heyn, M.P. (1982)Methods Enyzmol. 88:5-10.
Denisov, I.G., et al. (Mar. 2004) “Directed Self Assembly of Monodisperse Phospholipid Bilayer Nanodiscs with Controlled Size”;J. Am. Chem. Soc., In Press.
Duan, et al. (2004) Co-incorporation of Heterologously-ExpressedArabidopsisCytochrome P450 and P450 Reductase into Soluble Nanoscale Lipid Bilayers;Archives Biochemistry and Biophysics, In Press.
Durbin, D.M. and Jonas, A. (Dec. 1999) “Lipid-free apolipoproteins A-I and A-II promote remodeling of reconstituted high density lipoproteins and alter their reactivity with lecithin:cholesterol acyltransferase”J. Lipid Research40(12):2293-2302.
Dubois et al. (Jun. 2001) “Self-Assembly or Regular Hollow Icosahedra in Salt-Free Catanionic Solutions,”Nature411:672-675.
Fidge, N.H. (Feb. 1999) “High density lipoprotein receptors, binding proteins, and ligands”J. Lipid Research40(2):187-201.
Fielding, P.E. and Fielding, C.J. (1991) “Dynamics of lipoprotein transport in the circulatory system”Biochemistry of Lipids, Lipoproteins, and Membranes. D.E. Vance and J. Vance. Amsterdam, Elsevier Press Chapter 15, pp. 427-459.
Forte, T.M. et al. (1971) “Electron microscopic study on reassembly of plasma high density apoprotein with various lipids”Biochim. Biophys. Acta248:381-386.
Frank et al. (1998) “Importance of Central α-Helixes of Human Apolipoprotein A-1 in the Maturation of High Density Lipoproteins,”Biochem. 37(39):13902-13909.
Frank, P.G. et al. (1997) “Deletion of Central α-Helices in Human Apolipoprotein A-I: Effect on Phospholipid Association”Biochemistry36:1798-1806.
Friis, E.P. et al. (Feb. 1999) “An approach to long-range electron transfer mechanisms in mettalloproteins: in situ scanning tunneling ,microscopy with submolecular resolution”Proc. Natl. Acad. Sci. USA96:1379-1384.
Gillotte et al (1996) “Apolipoprotein A-I Structural Modification and the Functionality of Reconstituted High Density Lipoprotein Particles in Cellular Cholesterol Efflux,”J. Biol. Chem. 271(3):23792-23798.
Gillotte et al. (Jan. 1999) “Apolipoprotein-Mediated Plasma Membrane Microsolubilization. Role of Lipid Affinity and Membrane Penetration in the Efflux of Cellular Cholesterol and Phospholipid,”J. Biol. Chem. 274(4):2021-2028.
Glomset, J.A. (1968) “The plasma lecithin:cholesterol acyltransferase reaction”J. Lipid Research9:155-167.
Heyn, M.P. et al. (1982) “Reconstitution of Monomeric Bacteriorhodopsin into Phospholipid Vesicles;” Methods Enzymol. 88:31-35.
Holvoet, P. et al. (1995) “Phospholipid Binding and Lecithin-Cholesterol Acyltransferase Activation Propertie

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