34 results about "Disulphide bond formation" patented technology

Transgenic chloroplast technology could provide a viable solution to the production of Insulin-like Growth Factor I (IGF-I), Human Serum Albumin (HSA), or interferons (IFN) because of hyper-expression capabilities, ability to fold and process eukaryotic proteins with disulfide bridges (thereby eliminating the need for expensive post-purification processing). Tobacco is an ideal choice because of its large biomass, ease of scale-up (million seeds per plant), genetic manipulation and impending need to explore alternate uses for this hazardous crop. Therefore, all three human proteins will be expressed as follows: a) Develop recombinant DNA vectors for enhanced expression via tobacco chloroplast genomes b) generate transgenic plants c) characterize transgenic expression of proteins or fusion proteins using molecular and biochemical methods d) large scale purification of therapeutic proteins from transgenic tobacco and comparison of current purification / processing methods in E. coli or yeast e) Characterization and comparison of therapeutic proteins (yield, purity, functionality) produced in yeast or E. coli with transgenic tobacco f) animal testing and pre-clinical trials for effectiveness of the therapeutic proteins. Mass production of affordable vaccines can be achieved by genetically engineering plants to produce recombinant proteins that are candidate vaccine antigens. The B subunits of Enteroxigenic E. coli (LTB) and cholera toxin of Vibrio cholerae (CTB) are examples of such antigens. When the native LTB gene was expressed via the tobacco nuclear genome, LTB accumulated at levels less than 0.01% of the total soluble leaf protein. Production of effective levels of LTB in plants, required extensive codon modification. Amplification of an unmodified CTB coding sequence in chloroplasts, up to 10,000 copies per cell, resulted in the accumulation of up to 4.1% of total soluble tobacco leaf protein as oligomers (about 410 fold higher expression levels than that of the unmodified LTB gene). PCR and Southern blot analyses confirmed stable integration of the CTB gene into the chloroplast genome. Western blot analysis showed that chloroplast synthesized CTB assembled into oligomers and was antigenically identical to purified native CTB. Also, GM1-ganglioside binding assays confirmed that chloroplast synthesized CTB binds to the intestinal membrane receptor of cholera toxin, indicating correct folding and disulfide bond formation within the chloroplast. In contrast to stunted nuclear transgenic plants, chloroplast transgenic plants were morphologically indistinguishable from untransformed plants, when CTB was constitutively expressed. The introduced gene was stably inherited in the subsequent generation as confirmed by PCR and Southern blot analyses. Incrased production of an efficient transmucosal carrier molecule and delivery system, like CTB, in transgenic chloroplasts makes plant based oral vaccines and fusion proteins with CTB needing oral administration a much more practical approach.

Elimination of disulphide bond formation of cysteine-containing S.aureus antigens enhances antigen stability. The invention provides variant forms of cysteine-containing S.aureus antigen with a point mutation that replaces, deletes or modifies the cysteine residue.

Elimination of disulphide bond formation ofcysteine-containing S.aureus antigens enhances antigen stability. The invention provides a composition comprising variant forms of cysteine-containing S.aureus antigen with a point mutation that replaces, deletes or modifies the cysteine residue.

The invention provides the molecular degeneration of human growth hormone release hormone (HGHRH) peptides and its di clustering in the treatment of GH deficiency, infertility, dementia, diabetes, and enhanced immunity.The di agent of the present invention is two similar HGHRH -like peptide monomers that contain a single beurine molecular degeneration are connected by a sulfur (sulfurine formed by cysteine, and form an H -shaped structure (internal single ser → CYS inside the molecule → CYSreplace).The present invention also modifies the fatty acid chain of one of the lysine ε‑ amino groups of one of the lysine in the GHRH -like peptide.Extend the GHRH -like peptide monomer or di -polycatus in the body through fatty acid decoration, up to 17 days in the GH in the body.The present invention found that GHRH diodes with long -term activity have AIB → 2 ALA replacement, 18 C‑ 18 C formal sulfur formation, C20 fatty acid chain modification, and C -side amineization structure.

The invention discloses a long-acting recombinant human filaggrin expressed by Saccharomyces cerevisiae and its application. The nucleotide sequence of the long-acting recombinant human filaggrin is shown in Seq ID NO.1. The long-acting recombinant human filaggrin The amino acid sequence corresponding to the nucleotide sequence is shown in Seq ID NO.2. The amino acid sequence of long-acting recombinant human filaggrin includes the amino acid sequence of filaggrin and the amino acid sequence of human serum albumin. The amino acid sequence of filaggrin includes a monomer structure corresponding to the C-terminus of the filaggrin nucleotide sequence repeat amino acid sequence. The long-acting recombinant human filaggrin provided by the invention can promote the aggregation of keratin intermediate filaments and the formation of disulfide bonds between intermediate filaments, prevent the loss of epidermal water and the invasion of external allergic substances, and reduce the apoptosis of epidermal cells induced by ultraviolet rays sensitivity. The fusion of HAS effectively improves the stability of the recombinant protein.

The hybrid Fc proteins of this invention include IgG and IgM Fc components. The IgG Fc component includes at least a portion of a hinge region and CH2 and CHS regions. The IgM component includes C[mu]3 and C[mu]4 regions of a C[mu] constant region. The hybrid Fc proteins can form duplexes by interchain disulfide bonding between cysteines in their hinge regions. The hybrid Fc proteins can be used for treating immune disorders mediated by endogenous IgG, such as those previously treated with intravenous immunoglobulin.