Codon-optimized β-secretase and methods of refolding...

Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase

Reexamination Certificate

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

C536S023200, C435S320100, C435S252300, C435S254110, C435S419000, C435S325000, C435S252330

Reexamination Certificate

active

10443949

ABSTRACT:
The present application relates to methods for growing crystals of both the uncomplexed and complexed forms of β-secretase (BACE) polypeptide. Polypeptides used herein are derived from human BACE which is also known by the synonyms “mamapsin 2”, “human β-site APP-cleaving enzyme, and Asp2”. The present application also relates to crystalline forms of uncomplexed BACE and the three-dimensional structure of BACE, as determined from the crystals. In addition, the present application relates to the use of crystalline forms of BACE to identify ligands, preferably inhibitors (antagonists), which bind to, and preferably inhibit the enzymatic activity of, BACE. Furthermore, the present application relates to nucleic acid sequences encoding BACE polypeptide, and methods for making BACE in greater quantity than prior methods, resulting in more effective crystallization.

REFERENCES:
patent: 2001/0016324 (2001-08-01), Gurney et al.
patent: 2001/0044521 (2001-11-01), Lin
patent: 2002/0055459 (2002-05-01), Chopra et al.
patent: 2004/0014194 (2004-01-01), Beyer et al.
patent: WO 01/00663 (2001-01-01), None
patent: WO 01/00665 (2001-01-01), None
patent: WO 02/25276 (2002-03-01), None
patent: WO 03/12089 (2003-02-01), None
Witkowski et al., Biochemistry, vol. 38, pp. 11643-11650, 1999.
Lilie et al.,Curr. Opin. Biotech., vol. 9, pp. 497-501, 1998.
Hong et al., Science, vol. 290, pp. 150-153 (2000).
Lin et al., Proceedings Nat. Acad. Sci., vol. 97, No. 4, pp. 1456-1460 (2000).
Mallender et al., Mol. Pharm., vol. 59, No. 3, pp. 619-626 (2001).
Bennett et al., J. Biol. Chem, vol. 275, No. 48, pp. 37712-37717 (2000).
Bruinzeel et al., Prot. Exp. and Pur., vol. 26, pp. 139-148 (2002).
Creemers et al., J. Biol. Chem., vol. 276, No. 6, pp. 4211-4217 (2001).
Kennedy et al., Measuring human beta-secretase (BACE1) activity using homogeneous time-resolved fluorescence. Anal Biochem. Aug. 1, 2003;319(1):49-55.
Wang et al., Crystallization of glycosylated human BACE protease domain expressed in Trichoplusia ni. Biochim Biophys Acta. May 6, 2004;1698(2):255-9.
Vassar et al., Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science. Oct. 22, 1999;286(5440):735-41.
Sinha et al., Purification and cloning of amyloid precursor protein beta-secretase from human brain. Nature. Dec. 2, 1999;402(6761):537-40.
Hussain et al., Identification of a novel aspartic protease (Asp 2) as beta-secretase. Mol Cell Neurosci. Dec. 1999;14(6):419-27.
Lin et al., Human aspartic protease memapsin 2 cleaves the beta-secretase site of beta-amyloid precursor protein. Proc Natl Acad Sci U S A. Feb. 15, 2000;97(4):1456-60.
Creemers et al., Processing of beta-secretase by furin and other members of the proprotein convertase family. J Biol Chem. Feb. 9, 2001;276(6):4211-7.
Bennett et al., A furin-like convertase mediates propeptide cleavage of BACE, the Alzheimer's beta-secretase. J Biol Chem. Dec. 1, 2000;275(48):37712-7.
Esch et al., Cleavage of amyloid beta peptide during constitutive processing of its precursor. Science. Jun. 1, 1990;248(4959):1122-4.

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Codon-optimized β-secretase and methods of refolding... does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Codon-optimized β-secretase and methods of refolding..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Codon-optimized β-secretase and methods of refolding... will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-3766435

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.