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Extended recombinant polypeptides and compositions comprising same

By connecting the extended recombinant polypeptide XTEN with a bioactive protein to form a fusion protein, the instability and production complexity of bioactive proteins in aqueous solutions are solved, the half-life is extended, the solubility is improved, and the biological activity is enhanced, and production is simplified. process.

Active Publication Date: 2018-09-14
AMUNIX PHARMACEUTICALS INC
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

This is a time-consuming, inefficient, and expensive process that requires additional production steps and often complex purification operations

Method used

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Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0509] Embodiment 1: Construction of XTEN_AD36 motif segment

[0510] The following example describes the construction of a codon-optimized gene collection encoding a 36 amino acid motif. In the first step, a stuffer vector pCW0359 was constructed based on the pET vector, which contained the T7 promoter. pCW0359 encodes the cellulose binding domain (CBD) and the TEV isoflurane recognition site followed by a stuffer sequence. The stuffer sequence is flanked by BsaI, BbsI and KpnI sites. BsaI and BbsI sites were inserted such that they produced compatible overhangs after digestion. This stuffer sequence is followed by a truncated version of the GFP gene and a His tag. The stuffer sequence contains a stop codon, so E. coli cells carrying the stuffer plasmid pCW0359 form non-fluorescent colonies. The stuffer vector pCW0359 was digested with BsaI and KpnI to remove the stuffer segment and the resulting vector fragments were isolated by agarose gel purification. The sequence wa...

Embodiment 2

[0524] Example 2: Construction of the XTEN_AE36 segment

[0525] A codon library encoding XTEN sequences with a length of 36 amino acids was constructed. Name the XTEN sequence XTEN_AE36. Its segment has the amino acid sequence [X] 3 , wherein X is a 12mer peptide, the sequence is: GSPAGSPTSTEE (SEQ ID NO: 359), GSEPATSGSE TP (SEQ ID NO: 360), GTSESA TPESGP (SEQ ID NO: 361) or GTTEPSEGSAP (SEQ ID NO: 362). Inserts were obtained by annealing the following pairs of phosphorylated synthetic oligonucleotides:

[0526] AE1 for: AGGTAGCCCDGCWGGYTCTCCDACYTCYACYGARGA (SEQ ID NO: 363)

[0527] AE1rev: ACCTTCYTCRGTRGARGTHGGAGARCCWGCHGGGCT (SEQ ID NO: 364)

[0528] AE2 for: AGGTAGCGAACCKGCWACYTCYGGYTCTGARACYCC (SEQ ID NO: 365)

[0529] AE2rev: ACCTGGRGTYTCAGARCCRGARGTWGCMGGTTCGCT (SEQ ID NO: 366)

[0530] AE3 for: AGGTACYTCTGAAAGCGCWACYCCKGARTCYGGYCC (SEQ ID NO: 367)

[0531] AE3rev: ACCTGGRCCRGAYTCMGGRGTWGCGCTTTCAGARGT (SEQ ID NO: 368)

[0532] AE4 for: AGGTACYTCTACYGAACCKTCYGAR...

Embodiment 3

[0540] Example 3: Construction of the XTEN_AF36 segment

[0541] A codon library encoding sequences 36 amino acids in length was constructed. Name the sequence XTEN_AF36. Its segment has the amino acid sequence [X] 3 , wherein X is a 12mer peptide, the sequence is: GSTSESPSGTAP (SEQ ID NO: 447), GTSTPESGSASP (SEQ ID NO: 448), GTSPSGESSTAP (SEQ ID NO: 449) or GSTSSTAESPGP (SEQ ID NO: 450). Inserts were obtained by annealing the following pairs of phosphorylated synthetic oligonucleotides:

[0542] AF1 for: AGGTTCTACYAGCGAATCYCCKTCTGGYACYGCWCC (SEQ ID NO: 451)

[0543] AF1rev: ACCTGGWGCRGTRCCAGAMGGRGATTCGCTRGTAGA (SEQ ID NO: 452)

[0544] AF2 for: AGGTACYTCTACYCCKGAAAGCGGYTCYGCWTCTCC (SEQ ID NO: 453)

[0545] AF2rev: ACCTGGAGAWGCRGARCCGCTTTTCMGGRGTAGARGT (SEQ ID NO: 454)

[0546] AF3 for: AGGTACYTCYCCKAGCGGYGAATCTTCTACYGCWCC (SEQ ID NO: 455)

[0547] AF3rev: ACCTGGWGCRGTAGAAAGATTCRCCGCTMGGRGARGT (SEQ ID NO: 456)

[0548] AF4 for: AGGTTCYACYAGCTCTACYGCWGAATCTCCKGGYCC (SEQ...

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Abstract

The present invention relates to compositions comprising biologically active proteins linked to extended recombinant polypeptide (XTEN), isolated nucleic acids encoding the compositions and vectors and host cells containing the same, and methods of using such compositions in treatment of glucose-related diseases, metabolic diseases, coagulation disorders, and growth hormone-related disorders and conditions.

Description

[0001] This application is a divisional application of an invention patent application with an application date of February 3, 2010, an application number of 201080011467.6, and an invention title of "Extended Recombinant Polypeptide and Composition Comprising the Extended Recombinant Polypeptide". [0002] Statement Regarding Federally Funded Research [0003] This invention was made with government support under SBIR grant 2R44GM079873-02 awarded by the National Institutes of Health. The government has certain rights in this invention. [0004] Cross References to Related Applications [0005] This application claims U.S. Provisional Application Serial Nos. 61 / 149,669 filed February 3, 2009, 61 / 268,193 filed June 8, 2009, 61 / 185,112 filed June 8, 2009, August 24, 2009 61 / 236,493 filed on August 25, 2009, 61 / 243,707 filed on September 18, 2009, 61 / 245,490 filed on September 24, 2009, filed on November 10, 2009 61 / 280,955, 61 / 280,956 filed November 10, 2009, and 61 / 281,109...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): C07K19/00A61K38/26A61K38/20A61K38/48A61K38/27A61K38/36A61K38/17A61P3/10A61P3/04A61P5/10A61P3/06A61P9/14A61P1/00A61P7/04
CPCC07K14/001C07K2319/31C07K14/61C07K14/745C07K2319/35C12N9/6437C12N9/644C07K14/605A61P1/00A61P1/04A61P1/14A61P19/02A61P21/00A61P21/04A61P25/00A61P25/02A61P27/02A61P29/00A61P3/04A61P31/18A61P3/06A61P3/08A61P43/00A61P5/00A61P5/06A61P5/10A61P5/22A61P5/48A61P5/50A61P7/00A61P7/02A61P7/04A61P7/06A61P9/00A61P9/10A61P9/12A61P9/14A61P3/10A61K38/16C07K1/00C07K14/00C07K14/435C07K19/00C07K14/47C07K14/545
Owner AMUNIX PHARMACEUTICALS INC