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Details for Patent: 5,367,052

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Details for Patent: 5,367,052

Title: Amylin peptides
Abstract:A biologically active peptide associated with diabetes and designated herein "amylin" and processes for preparing it and assaying for it and for Type 2 diabetes are disclosed. The invention includes peptides having the amino acid sequence KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY, substantially homologous sequences of amino acids, proamylin, as well as biologically active subfragments and conservative mutations. The peptide may be prepared from diabetic pancreata by solubilization of amyloid and isolation of the peptide by gel filtration and reverse phase chromotography. Amylin may also be synthesized, or it may be produced by recombinant DNA techniques using the disclosed nucleic acid sequences.
Inventor(s): Cooper; Garth J. S. (Solana Beach, CA), Willis; Antony C. (Witney, GB2)
Assignee: Amylin Pharmaceuticals, Inc. (San Diego, CA)
Filing Date:May 01, 1989
Application Number:07/346,624
Claims:1. An amylin peptide having thirty-seven amino acids, in which the C-terminal tyrosine of said peptide is carboxyamidated, said peptide contains an intramolecular linkage between cysteine resides at positions 2 and 7, and wherein said peptide is capable of reducing insulin-induced incorporation of glucose into glycogen in isolated rat soleus muscle.

2. The amylin peptide KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY which contains an intramolecular linkage between the cysteine residues at positions 2 and 7, and wherein the C-terminal tyrosine is carboxyamidated.

3. A process for the preparation of an amylin peptide as recited in claim 2, comprising the steps of (a) preparing solubilized amyloid by use of formic acid in conjunction with ultrasound, (b) subjecting the amyloid material from step (a) to normal phase high performance liquid chromatography gel filtration using a mobile phase comprising aqueous guanidine and sodium phosphate, and (c) subjecting the amyloid material from step (b) to high performance liquid chromatography using a mobile phase comprising triflouracetic acid and elution by acetonitrile.

4. A substantially pure amylin peptide prepared by the process of claim 3.

5. An amylin peptide as recited in claim 1 or 2 which is at least about 50% pure.

6. An amylin peptide as recited in claim 1 or 2 which is at least about 80% pure.

7. An amylin peptide as recited in claim 1 or 2 which is at least about 90% pure.

8. An amylin peptide as recited in claim 1 or 2 which is at least about 95% pure.

9. An amylin peptide as recited in claim 1 or 2 which is at least about 99% pure.

10. The amylin peptide of claim 4 wherein said amylin peptide is an amylin peptide having thirty-seven amino acids, in which the C-terminal tyrosine of said peptide is carboxyamidated. said peptide contains an intramolecular linkage between the cysteine residues at positions 2 and 7, and wherein said peptide is capable of reducing insulin-induced incorporation of glucose into glycogen in isolated rat soleus muscle.

11. The amylin peptide of claim 5 wherein said amylin peptide is an amylin peptide having thirty-seven amino acids, in which the C-terminal tyrosine of said peptide is carboxyamidated, said peptide contains an intramolecular linkage between the cysteine residues at positions 2 and 7, and wherein said peptide is capable of reducing insulin-induced incorporation of glucose into glycogen in isolated rat soleus muscle.

12. The amylin peptide of claim 6 wherein said amylin peptide is an amylin peptide having thirty-seven amino acids, in which the C-terminal tyrosine of said peptide is carboxyamidated, said peptide contains an intramolecular linkage between the cysteine residues at positions 2 and 7, and wherein said peptide is capable of reducing insulin-induced incorporation of glucose into glycogen in isolated rat soleus muscle.

13. The amylin peptide of claim 7 wherein said amylin peptide is an amylin peptide havng thirty-seven amino acids, in which the C-terminal tyrosine of said peptide is carboxyamidated, said peptide contains an intramolecular linkage between the cysteine residues at positions 2 and 7, and wherein said peptide is cabable of reducing insulin-induced incorporation of glucose into glycogen in isolated rat soleus muscle.

14. The amylin peptide of claim 8 wherein said amylin peptide is an amylin peptide having thirty-seven amino acids, in which the C-terminal tyrosine of said peptide is carboxyamidated, said peptide contains an intramolecular linkage between the cysteine residues at positions 2 and 7, and wherein said peptide is capable of reducing insulin-induced incorporation of glucose into glycogen in isolated rat soleus muscle.

15. The amylin peptide of claim 9 wherein said amylin peptide is an amylin peptide having thirty-seven amino acids, in which the C-terminal tyrosine of said peptide is carboxyamidated, said peptide contains an intramolecular linkage between the cysteine residues at positions 2 and 7, and wherein said peptide is capable of reducing insulin-induced incorporation of glucose into glycogen in isolated rat soleus muscle.

16. The amylin peptide of claim 4 wherein said amylin peptide is the amylin peptide KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY which contains an intramolecular linkage between the cysteine residues at positions 2 and 7, and wherein the C-terminal tyrosine is carboxyamidated.

17. The amylin peptide of claim 5 wherein said amylin peptide is the amylin peptide KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY which contains an intramolecular linkage between the cysteine residues at positions 2 and 7, and wherein the C-terminal tyrosine is carboxyamidated.

18. The amylin peptide of claim 6 wherein said amylin peptide is the amylin peptide KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY which contains an intramolecular linkage between the cysteine residues at positions 2 and 7, wherein the C-terminal tyrosine is carboxyamidated.

19. The amylin peptide of claim 7 wherein said amylin peptide is the amylin peptide KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY which contains an intramolecular linkage between the cysteine residues at positions 2 and 7, wherein the C-terminal tyrosine is carboxyamidated.

20. The amylin peptide of claim 8 wherein said amylin peptide is the amylin peptide KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY which contains an intramolecular linkage between the cysteine residues at positions 2 and 7, wherein the C-terminal tyrosine is carboxyamidated.

21. The amylin peptide of claim 9 wherein said amylin peptide is the amylin peptide KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY which contains an intramolecular linkage between the cysteine residues at positions 2 and 7, wherein the C-terminal tyrosine is carboxyamidated.
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