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Title: US5231011: Segregated folding determinants for small disulfide-rich peptides
[ Derwent Title ]


Country: US United States of America

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15 pages

 
Inventor: Hillyard, David R.; Holliday, UT
Olivera, Baldomero M.; Salt Lake City, UT

Assignee: University of Utah, Salt Lake City, UT
other patents from UNIVERSITY OF UTAH (600055) (approx. 249)
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Published / Filed: 1993-07-27 / 1991-04-18

Application Number: US1991000689693

IPC Code: Advanced: C07K 1/113; C07K 14/435; C12P 21/06;
Core: C07K 1/00; more...
IPC-7: C07K 7/00; C07K 15/00; C12P 21/00; C12P 21/06;

U.S. Class: Current: 435/069.7; 435/068.1; 435/069.1; 435/480; 435/488; 530/300; 530/333; 530/334; 530/338; 530/350; 530/857;
Original: 435/069.7; 435/068.1; 435/069.1; 435/172.3; 530/333; 530/300; 530/334; 530/338; 530/857; 530/350;

Field of Search: 530/333,350,300,334,338,857 435/68.1,69.7,69.1,172.3

Government Interest:     This invention was made with government support under Contract No. N00014-88-K-0178 awarded by the Department of the Navy and under Contract No. GM-22737 awarded by the Department of Health and Human Services. The government has certain rights in the invention.

Priority Number:
1991-04-18  US1991000689693

Abstract: The preparation of small peptides with multiple disulfide bonds is accomplished by forming a prepropeptide with an N-terminal excised region separated from the cysteine-rich peptide by one or more cleavable amino acid residues. The excised region preferably consists of an N-terminal end providing a hydrophobic signal sequence domain having up to approximately 25 amino acids, and an intermediate central propeptide domain having a variable length of between about 5-50 amino acids. The N-terminal excised region serves as a folding template to direct the formation of specific disulfide bonds in the cysteine-rich peptide. The cysteine-rich peptide is cleaved by enzymes releasing the biologically active peptide.

Attorney, Agent or Firm: Thorpe, North & Western ;

Primary / Asst. Examiners: Wax, Robert A.; Hendricks, Keith D.

Maintenance Status: E3 Expired  Check current status

INPADOC Legal Status: Show legal status actions

Family: None

First Claim:
Show all 13 claims
What is claimed is:     1. A method of forming a mature biologically active cysteine-rich peptide having specific disulfide bonds between cysteine residues providing a consistent folding pattern which comprises the formation, by cloning methods, solution phase synthesis or solid phase synthesis, or a combination of solution phase synthesis and solid phase synthesis, of a prepropeptide consisting of a C-terminal excised region separated from said cysteine-rich peptide by one or more cleavable amino acid residues wherein the sequence of the N-terminal excised region is derived from conotoxin peptides found in Conus venom and serves as a folding template to direct the formation of said specific disulfide bonds in said cysteine-rich peptide, and then cleaving said mature peptide form said prepropeptide.

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Forward References: Show 10 U.S. patent(s) that reference this one

       
U.S. References: Go to Result Set: All U.S. references   |  Forward references (10)   |   Backward references (0)   |   Citation Link

       
Foreign References: None

Other References:
  • Olivera et al. (1990) Science, vol. 249, Jul. 1990, pp. 257-263. (7 pages) Cited by 36 patents
  • Olivera et al. (1987), Biochemistry, vol. 26, No. 8, 1987, pp. 2086-2090. (5 pages) Cited by 19 patents
  • Woodward et al., Eubo Journal, vol. 9, No. 4, pp. 1015-1020, 1990.
  • Becker et al., Eur. J. Biochem, vol. 185, 1989, pp. 79-84. (6 pages) Cited by 7 patents
  • Hillyard et al., Biochemistry, vol. 28, No. 1, 1989, pp. 358-361. (4 pages) Cited by 13 patents
  • Cruz et al., Biochemistry, vol. 28, No. 8, 1989, pp. 3437-3442. (6 pages) Cited by 9 patents


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