Get our Free Patent Expiration Newsletter

Serving leading biopharmaceutical companies globally:

Moodys
Medtronic
Johnson and Johnson
Boehringer Ingelheim
Express Scripts
McKesson

Last Updated: February 16, 2020

DrugPatentWatch Database Preview

Claims for Patent: 7,501,484

See Plans and Pricing

« Back to Dashboard

Summary for Patent: 7,501,484
Title:Methods and DNA constructs for high yield production of polypeptides
Abstract: The invention provides an inclusion body fusion partner to increase peptide and polypeptide production in a cell.
Inventor(s): Williams; James A. (Lincoln, NE), Luan; Peng (Fishers, IN), Xia; Yuannan (Lincoln, NE), Harley; Scott (Pensacola, FL)
Assignee: Restoragen, Inc (Lincoln, NE)
Application Number:10/997,078
Patent Claims:1. A polypeptide comprising in tandem: a) a first region comprising an inclusion body fusion partner having an amino acid sequence comprising SEQ ID NO: 2; and b) a second region not naturally associated with the first region comprising a preselected amino acid sequence selected from the group consisting of amino acids 7-36 of GLP-1 (SEQ ID NO: 31), amino acids 7-36 of GLP-1 (SEQ ID NO: 31) further consisting of an amide linkage at the C-terminus, amino acids 7-37 of GLP-1 (SEQ ID NO: 32), amino acids 7-37 of GLP-1 (SEQ ID NO: 32) further consisting of an amide linkage at the C-terminus, amino acids 7-36 of GLP-1 further consisting of a K to R substitution at position 26 (SEQ ID NO: 33), amino acids 7-36 of GLP-1 further consisting of a K to R substitution at position 26 (SEO ID NO:33) and further consisting of an amide linkage at the C-terminus, amino acids 7-37 of GLP-1 further consisting of a K to R substitution at position 26 (SEQ ID NO: 34), amino acids 7-37 of GLP-1 further consisting of a K to R substitution at position 26 SE ID NO:34 and further consisting of an amide linkage at the C-terminus (SEQ ID NO: 34), amino acids 1-34 of GLP-2 (SEQ ID NO: 35), amino acids 1-34 of GLP-2 (SEQ ID NO: 35) and further consisting of an amide linkage at the C-terminus, amino acids 1-33 of GLP-2 (SEQ ID NO: 36), amino acids 1-33 of GLP-2 (SEQ ID NO: 36) and further consisting of an amide linkage at the C-terminus, amino acids 1-33 of GLP-2 further consisting of an A to G substitution at position 2 (SEQ ID NO: 37), amino acids 1-33 of GLP-2 further consisting of an A to G substitution at position 2 (SEQ ID NO: 37) and further consisting of an amide linkage at the C-terminus, amino acids 1-34 of GLP-2 further consisting of an A to G substitution at position 2 (SEQ ID NO: 38), amino acids 1-34 of GLP-2 further consisting of an A to G substitution at position 2 (SEQ ID NO: 38) and further consisting of an amide linkage at the C-terminus, amino acids 1-44 of GRF (SEQ ID NO: 39), amino acids 1-34 of (SEQ ID NO: 40), amino acids 1-37 of PTH (SEQ ID NO: 41), amino acids 1-84 of PTH (SEQ ID NO: 42), amino acids 27-38 of Amyloid P Component (SEQ ID NO: 43) and further consisting of an amide linkage at the C-terminus, (Tyr0)-Fibrinopeptide A (SEQ ID NO: 44), Urechistachykinin II (SEQ ID NO: 45), amino acids 12-28 of Amyloid .beta.-Protein (SEQ ID NO: 46), amino acids 22-35 of Amyloid .beta.-Protein (SEQ ID NO: 47), camel .beta.-Endorphin (SEQ ID NO: 48), porcine Valosin (SEQ ID NO: 49), and mouse Vasoactive Intestinal Contractor Peptide (SEQ ID NO: 50).

2. The polypeptide according to claim 1, wherein the first region is linked to the N-terminus of the second region.

3. The polypeptide according to claim 1, wherein the first region is linked to the C-terminus of the second region.

4. The polypeptide according to claim 1, further comprising a cleavable peptide linker between the first region and the second region.

5. The polypeptide of claim 4, wherein the cleavable peptide linker can be cleaved by a cleavage agent selected from the group consisting of palladium, cyanogen bromide, Clostripain, Thrombin, Trypsin, Trypsin-like protease, Carboxypeptidase, Enterokinase, Kex 2 protease, Omp T protease, Factor Xa protease, Subtilisin, HIV protease, Rhinovirus protease, Furilisin protease, IgA protease, Human Pace protease, Collagenase, Plum pox potyvirus Nia protease, Poliovirus 2Apro protease, Poliovirus 3C protease, Nia protease, Genenase, Furin Chymotrypsin, Elastase, Subtilisin, Proteinase K, Pepsin, Rennin, microbial aspartic proteases, Papain, Ficin, Bromelain, Collagenase, Thermolysin, Endoprotease Arg-C, Endoprotease Glu-C, Endoprotease Lys-C, Kallikrein and Plasmin.

6. The polypeptide according to claim 4, wherein the cleavable peptide linker is cleaved by a tissue specific protease.

7. The polypeptide according to claim 6, wherein the tissue specific protease is a prostate specific antigen.

8. The polypeptide according to claim 4, wherein the cleavable peptide linker between the first region and the second region is selected from the group consisting of Ala-Phe-Leu-Gly-Pro-Gly-Asp-Arg (SEQ ID NO: 71), Val-Asp-Asp-Arg (SEQ ID NO: 72), Gly-Ser-Asp-Arg (SEQ ID NO: 73), Ile-Thr-Asp-Arg (SEQ ID NO: 74) and Pro-Gly-Asp-Arg (SEQ ID NO: 75).

9. The polypeptide according to claim 1, further comprising a fusion tag.

10. The polypeptide according to claim 9, wherein the fusion tag is a ligand for a cellular receptor.

11. The polypeptide according to claim 10, wherein the fusion tag is insulin.

12. The polypeptide according to claim 9, wherein the fusion tag is a .beta.-gal a GST a CAT a TrpE, a staphylococcal protein A, a streptococcal protein, a maltose binding protein, a starch binding protein, a cellulose-binding domain of endoglucanase A, a cellulose binding domain of exoglucanase Cex, a Biotin-binding domain, a recA, a Flag, a poly(Arg), a Poly(Asp), a Glutamine, a poly(His), a poly(Phe), a poly(Cys), a green fluorescent protein, a red fluorescent protein, a yellow fluorescent protein, a cayenne fluorescent protein, a biotin, an avidin, a streptavidin, or an antibody epitope.

13. The tandem polypeptide of claim 9, wherein the fusion tag is linked to the preselected amino acid sequence.

14. The polypeptide of claim 13, farther comprising a cleavable peptide linker between the preselected amino acid sequence and the fusion tag.

15. The polypeptide of claim 14, wherein the cleavable peptide linker can be cleaved by a cleavage agent selected from the group consisting of palladium, cyanogen bromide, Clostripain, Thrombin , Trypsin, Trypsin-like protease, Carboxypeptidase, Enterokinase, Kex 2 protease, Omp T protease, Factor Xa protease, Subtilisin, HIV protease; Rhinovirus protease, Furilisin protease, IgA protease, Human Pace protease, Collagenase, Plum pox potyvirus Nia protease, Poliovirus 2Apro protease, Poliovirus 3C protease, Nia protease, Genenase, Furin, Chymotrypsin, Elastase, Proteinase K, Pepsin, Rennin, microbial aspartic proteases, Papain, Ficin, Bromelain, Collagenase, Thermolysin, Endoprotease Arg-C, Endoprotease Glu-C, Endoprotease Lys-C, Kallikrein and Plasmin.

16. The polypeptide according to claim 1, further comprising an additional sequence selected from the group consisting of DYKDDDDK (SEQ ID NO: 81) and MASMTGGQQMGR (SEQ ID NO: 83).

17. An amino acid sequence comprising SEQ ID NO: 83 and SEQ ID NO: 2.

Details for Patent 7,501,484

Applicant Tradename Biologic Ingredient Dosage Form BLA Number Approval Date Patent No. Assignee Estimated Patent Expiration Status Orphan Source
Smith And Nephew SANTYL collagenase OINTMENT;TOPICAL 101995 001 1965-06-04   Start Trial Restoragen, Inc (Lincoln, NE) 2022-05-24 RX search
>Applicant >Tradename >Biologic Ingredient >Dosage Form >BLA >Number >Approval Date >Patent No. >Assignee >Estimated Patent Expiration >Status >Orphan >Source

Make Better Decisions: Try a trial or see plans & pricing

Serving leading biopharmaceutical companies globally:

Boehringer Ingelheim
Moodys
Mallinckrodt
McKesson
Harvard Business School
Express Scripts

Drugs may be covered by multiple patents or regulatory protections. All trademarks and applicant names are the property of their respective owners or licensors. Although great care is taken in the proper and correct provision of this service, thinkBiotech LLC does not accept any responsibility for possible consequences of errors or omissions in the provided data. The data presented herein is for information purposes only. There is no warranty that the data contained herein is error free. thinkBiotech performs no independent verifification of facts as provided by public sources nor are attempts made to provide legal or investing advice. Any reliance on data provided herein is done solely at the discretion of the user. Users of this service are advised to seek professional advice and independent confirmation before considering acting on any of the provided information. thinkBiotech LLC reserves the right to amend, extend or withdraw any part or all of the offered service without notice.