WO2007086879A2 - Method of expressing proteins with disulfide bridges - Google Patents

Method of expressing proteins with disulfide bridges Download PDF

Info

Publication number
WO2007086879A2
WO2007086879A2 PCT/US2006/004413 US2006004413W WO2007086879A2 WO 2007086879 A2 WO2007086879 A2 WO 2007086879A2 US 2006004413 W US2006004413 W US 2006004413W WO 2007086879 A2 WO2007086879 A2 WO 2007086879A2
Authority
WO
WIPO (PCT)
Prior art keywords
disintegrin
protein
domain
sequence
thioredoxin
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Ceased
Application number
PCT/US2006/004413
Other languages
English (en)
French (fr)
Other versions
WO2007086879A3 (en
Inventor
Radu Minea
Frances Markland
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
University of Southern California USC
Original Assignee
University of Southern California USC
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by University of Southern California USC filed Critical University of Southern California USC
Priority to EP13157149.9A priority Critical patent/EP2634252B1/en
Priority to CA002597647A priority patent/CA2597647A1/en
Priority to JP2007556197A priority patent/JP2008536479A/ja
Priority to EP06849695A priority patent/EP1856255A4/en
Priority to AU2006336468A priority patent/AU2006336468B2/en
Publication of WO2007086879A2 publication Critical patent/WO2007086879A2/en
Anticipated expiration legal-status Critical
Publication of WO2007086879A3 publication Critical patent/WO2007086879A3/en
Ceased legal-status Critical Current

Links

Classifications

    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P21/00—Preparation of peptides or proteins
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • A61K38/1703—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P35/00—Antineoplastic agents
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P35/00—Antineoplastic agents
    • A61P35/04—Antineoplastic agents specific for metastasis
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P7/00—Drugs for disorders of the blood or the extracellular fluid
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P7/00—Drugs for disorders of the blood or the extracellular fluid
    • A61P7/02—Antithrombotic agents; Anticoagulants; Platelet aggregation inhibitors
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
    • C07K14/24—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Enterobacteriaceae (F), e.g. Citrobacter, Serratia, Proteus, Providencia, Morganella, Yersinia
    • C07K14/245—Escherichia (G)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
    • C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
    • C12N9/6402—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from non-mammals
    • C12N9/6418—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from non-mammals from snakes
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/90—Isomerases (5.)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P21/00—Preparation of peptides or proteins
    • C12P21/02—Preparation of peptides or proteins having a known sequence of two or more amino acids, e.g. glutathione
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2319/00—Fusion polypeptide
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2319/00—Fusion polypeptide
    • C07K2319/20—Fusion polypeptide containing a tag with affinity for a non-protein ligand
    • C07K2319/21—Fusion polypeptide containing a tag with affinity for a non-protein ligand containing a His-tag
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2319/00—Fusion polypeptide
    • C07K2319/50—Fusion polypeptide containing protease site
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2319/00—Fusion polypeptide
    • C07K2319/90—Fusion polypeptide containing a motif for post-translational modification

Definitions

  • CN also has the ability to directly engage tumor cells and suppress their growth in a cytostatic manner (Trikha, De Clerck et al. 1994; Trikha, Rote et al. 1994; Schmitmeier, Markland et al. 2000).
  • the antitumoral activity of CN is based on its high affinity interaction with integrins ⁇ 5 ⁇ l, ⁇ v ⁇ 3 and ⁇ v ⁇ 5 on both cancer cells and newly growing vascular endothelial cells (Trikha, De Clerck et al.
  • FIG. 18B shows a mutated CN gene sequence after replacing all CGG and most ACA rarely used codons. The ACA codons left unreplaced are highlighted in bold.
  • FIG. 19 is a map of the pCDFDuet- 1 vector (from Novagen) .
  • bacterial host cells may be engineered to cytoplasmically express a disulfide isomerase normally targeted to the periplasmic space of the host.
  • the disulfide isomerase is DsbC.
  • DsbC disulfide isomerase
  • DsbC is specifically activated by the periplasmic N-terminal domain (DsbD ⁇ -domain) of the transmembrane electron transporter DsbD.
  • DsbA and DsbC the formation of protein disulfide bonds is catalyzed by DsbA and DsbC.
  • the oxidation pathway consists of DsbA, a powerful oxidase (the most oxidizing protein known) and its modulator, DsbB, that couples DsbA with the respiratory chain (in aerobic conditions) or with the anaerobic electron acceptors (in anaerobic conditions).
  • HPLC purified rCN and VN were recognized by a polyclonal antisera raised against native CN in both ELISA and Western blotting assays (data not shown).
  • Biological activity of liposome encapsulated CN was evaluated as previously described (Swenson, Costa et al. 2004). Briefly, three groups of five nude mice had MDA-MB-435 human mammary carcinoma cells implanted in the mammary fat pad. Two weeks following implantation, small tumors were palpable and treatment was commenced. Animals were treated with LCN or LVN (105 ⁇ g, twice weekly, i.v. administration); a PBS treated control was included. A significant inhibitory effect on tumor growth by LVN was observed (FIG. 12). The functional activity of VN was indicated by its in vivo cancer therapeutic effect, which was found to be similar to native CN.
  • FIG. 15A shows a big peak of 13507.0, for CN representing the dimer, and two smaller peaks probably CN from which a single amino acid has been cleaved.
  • FIG. 15B shows a single peak of 7146.0, for VN, confirming that it is a monomer.
  • Trxback Trx reverse external primer introducing the BgIII restriction site and designed for inserting the 3' end of the active site mutants into pET32a vector: 5'TACCCAGATCTGGGCTGTCCATGTGCTS' (SEQ ID NO: 24)
  • DsbCGFfor - active site mutated DsbC (CGFC) overlap extension forward primer: 5'TTTACTGATATTACCTGTGGTTTCTGCCACAAACTGCATGAGS' (SEQ ID NO: 36)

Landscapes

  • Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Organic Chemistry (AREA)
  • Engineering & Computer Science (AREA)
  • General Health & Medical Sciences (AREA)
  • Zoology (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Wood Science & Technology (AREA)
  • Genetics & Genomics (AREA)
  • Medicinal Chemistry (AREA)
  • Biochemistry (AREA)
  • Molecular Biology (AREA)
  • General Chemical & Material Sciences (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Microbiology (AREA)
  • General Engineering & Computer Science (AREA)
  • Biotechnology (AREA)
  • Animal Behavior & Ethology (AREA)
  • Veterinary Medicine (AREA)
  • Public Health (AREA)
  • Pharmacology & Pharmacy (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Biomedical Technology (AREA)
  • Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
  • Gastroenterology & Hepatology (AREA)
  • Biophysics (AREA)
  • Marine Sciences & Fisheries (AREA)
  • Diabetes (AREA)
  • Hematology (AREA)
  • Immunology (AREA)
  • Epidemiology (AREA)
  • Oncology (AREA)
  • Peptides Or Proteins (AREA)
  • Micro-Organisms Or Cultivation Processes Thereof (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)
  • Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
PCT/US2006/004413 2005-02-11 2006-02-09 Method of expressing proteins with disulfide bridges Ceased WO2007086879A2 (en)

Priority Applications (5)

Application Number Priority Date Filing Date Title
EP13157149.9A EP2634252B1 (en) 2005-02-11 2006-02-09 Method of expressing proteins with disulfide bridges
CA002597647A CA2597647A1 (en) 2005-02-11 2006-02-09 Method of expressing proteins with disulfide bridges
JP2007556197A JP2008536479A (ja) 2005-02-11 2006-02-09 ジスルフィド架橋を有するタンパク質の発現法
EP06849695A EP1856255A4 (en) 2005-02-11 2006-02-09 PROCESS FOR EXPRESSING PROTEINS VIA DISULPHIDE BRIDGES
AU2006336468A AU2006336468B2 (en) 2005-02-11 2006-02-09 Method of expressing proteins with disulfide bridges

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
US65252905P 2005-02-11 2005-02-11
US60/652,529 2005-02-11

Publications (2)

Publication Number Publication Date
WO2007086879A2 true WO2007086879A2 (en) 2007-08-02
WO2007086879A3 WO2007086879A3 (en) 2009-06-11

Family

ID=38309637

Family Applications (1)

Application Number Title Priority Date Filing Date
PCT/US2006/004413 Ceased WO2007086879A2 (en) 2005-02-11 2006-02-09 Method of expressing proteins with disulfide bridges

Country Status (7)

Country Link
US (4) US7754850B2 (cg-RX-API-DMAC7.html)
EP (2) EP1856255A4 (cg-RX-API-DMAC7.html)
JP (1) JP2008536479A (cg-RX-API-DMAC7.html)
CN (1) CN101535492A (cg-RX-API-DMAC7.html)
AU (1) AU2006336468B2 (cg-RX-API-DMAC7.html)
CA (1) CA2597647A1 (cg-RX-API-DMAC7.html)
WO (1) WO2007086879A2 (cg-RX-API-DMAC7.html)

Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN108864291A (zh) * 2011-11-23 2018-11-23 拜奥文斯瑞有限公司 重组蛋白及其治疗用途
EP3505532A4 (en) * 2016-08-25 2020-04-22 Nexgen Biotechnologies, Inc. SCORPION POISON FUSION PROTEIN WITH IMPROVED EFFECT IN THE PROLIFERATION OF SKIN CELLS AND COSMETIC COMPOSITION, THEREFORE AS AN ACTIVE SUBSTANCE TO REDUCE SKIN WRINKLES, TO IMPROVE THE SKIN ELASTICITY AND TO PREVENT THE AGE

Families Citing this family (21)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CA2597647A1 (en) 2005-02-11 2007-08-02 University Of Southern California Method of expressing proteins with disulfide bridges
EP2029156A4 (en) * 2006-05-01 2010-07-21 Univ Southern California COMBINATION THERAPY FOR CANCER TREATMENT
US7943728B2 (en) * 2006-12-26 2011-05-17 National Cheng Kung University Disintegrin variants and their use in treating osteoporosis-induced bone loss and angiogenesis-related diseases
US8802394B2 (en) 2008-11-13 2014-08-12 Radu O. Minea Method of expressing proteins with disulfide bridges with enhanced yields and activity
US8470554B2 (en) * 2008-12-22 2013-06-25 St. Jude Children's Research Hospital Prokaryotic expression of soluble, active Dkk
EP2534171A4 (en) 2010-02-11 2013-07-17 Univ Southern California MODIFIED ADAM DISINTEGRIN DOMAIN POLYPEPTIDES AND USES THEREOF
CN102154336A (zh) * 2011-01-25 2011-08-17 国家海洋局第三海洋研究所 嗜酸硫化芽孢杆菌硫氧还蛋白还原酶基因及其重组蛋白
EP2527424A1 (en) * 2011-05-26 2012-11-28 Richter-Helm Bio Tec GmbH & Co. KG Recombinant expression of soluble Interferon
US20170054032A1 (en) 2015-01-09 2017-02-23 SanDisk Technologies, Inc. Non-volatile memory having individually optimized silicide contacts and process therefor
CN105039377A (zh) * 2015-08-24 2015-11-11 武汉真福医药股份有限公司 溶栓酶基因qk-02的表达方法及专用表达载体和工程菌
EP3373948A4 (en) * 2015-11-13 2019-04-17 University of Southern California RADIOMARKED DISINTER GRINDER AS BRACHYTHERAPY AGENT
US10258567B1 (en) 2016-11-17 2019-04-16 Grace Procurements Llc Vaginal probiotic products and related processes
CN107384934A (zh) * 2017-08-18 2017-11-24 安徽安科生物工程（集团）股份有限公司 重组人干扰素α2b的制备方法
US11169583B2 (en) * 2018-08-07 2021-11-09 Western Digital Technologies, Inc. Methods and apparatus for mitigating temperature increases in a solid state device (SSD)
CN113286810A (zh) * 2018-09-25 2021-08-20 Absci有限责任公司 蛋白质纯化方法
ES2944837T3 (es) * 2018-11-08 2023-06-26 Sutro Biopharma Inc Cepas de E. coli con citoplasma oxidativo
US12351850B2 (en) 2020-04-30 2025-07-08 Sutro Biopharma, Inc. Methods of producing full-length antibodies using E. coli
CN114107353B (zh) * 2021-10-29 2024-07-23 成都佩德生物医药有限公司 一种高效表达多肽毒素的质粒及其制备方法与应用
EP4361172A3 (en) 2022-10-27 2024-05-29 Science4Beauty Sp. z o.o. Expression vector for recombinant u-conotoxin tiiia or tiiialamut expression in e.coli
CN117756949B (zh) * 2024-02-21 2024-10-15 中国人民解放军军事科学院军事医学研究院 一种正痘病毒属融合抗原及应用
CN120118913B (zh) * 2025-05-14 2025-09-02 中国科学院苏州纳米技术与纳米仿生研究所 一种编码人防御素的核酸分子及制备人防御素方法和应用

Family Cites Families (109)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US4610879A (en) 1984-01-06 1986-09-09 University Of Southern California Fibrinolytic enzyme from snake vernom
US5066592A (en) 1988-03-08 1991-11-19 Temple University Of The Commonwealth System Of Higher Education Trigramin - a platelet aggregation inhibiting polypeptide
US6133029A (en) 1988-03-21 2000-10-17 Chiron Corporation Replication defective viral vectors for infecting human cells
US5703055A (en) 1989-03-21 1997-12-30 Wisconsin Alumni Research Foundation Generation of antibodies through lipid mediated DNA delivery
US5278324A (en) 1990-08-28 1994-01-11 Virginia Tech Intellectual Properties, Inc. Water soluble derivatives of taxol
US5227400A (en) 1991-09-23 1993-07-13 Florida State University Furyl and thienyl substituted taxanes and pharmaceutical compositions containing them
US5250683A (en) 1991-09-23 1993-10-05 Florida State University Certain substituted taxanes and pharmaceutical compositions containing them
US5272171A (en) 1992-02-13 1993-12-21 Bristol-Myers Squibb Company Phosphonooxy and carbonate derivatives of taxol
US5248796A (en) 1992-06-18 1993-09-28 Bristol-Myers Squibb Company Taxol derivatives
US5254580A (en) 1993-01-19 1993-10-19 Bristol-Myers Squibb Company 7,8-cyclopropataxanes
FR2705686B1 (fr) 1993-05-28 1995-08-18 Transgene Sa Nouveaux adénovirus défectifs et lignées de complémentation correspondantes.
US6080569A (en) 1993-06-24 2000-06-27 Merck & Co., Inc. Adenovirus vectors generated from helper viruses and helper-dependent vectors
US5731288A (en) 1993-10-22 1998-03-24 University Of Southern California Compositions containing contortrostatin and methods for the use thereof
US7220724B2 (en) 1993-10-22 2007-05-22 University Of Southern California Contortrostatin CN and methods for its use in preventing metastasis and other conditions
US5814609A (en) 1993-10-22 1998-09-29 University Of Southern California Compositions containing a disintegrin and methods for its use in preventing metastasis and other conditions
US6710030B1 (en) * 1993-10-22 2004-03-23 University Of Southern California Contortrostain (CN) and methods for its use in preventing metastasis and other conditions
US20030186884A1 (en) 2000-06-08 2003-10-02 Markland Francis S. Contortrostatin (CN) and methods for its use in preventing metastasis and other conditions
US5658785A (en) 1994-06-06 1997-08-19 Children's Hospital, Inc. Adeno-associated virus materials and methods
FR2725726B1 (fr) 1994-10-17 1997-01-03 Centre Nat Rech Scient Vecteurs viraux et utilisation en therapie genique
US5641665A (en) 1994-11-28 1997-06-24 Vical Incorporated Plasmids suitable for IL-2 expression
US6040295A (en) 1995-01-13 2000-03-21 Genemedicine, Inc. Formulated nucleic acid compositions and methods of administering the same for gene therapy
ES2161362T3 (es) 1995-05-22 2001-12-01 Us Gov Health & Human Serv Vectores retroviricos procedentes de virus de la leucosis del sarcoma aviar que permiten la transferencia de genes a celulas de mamiferos, y usos terapeuticos de los mismos.
AU5253998A (en) 1996-11-13 1998-06-03 Board Of Regents, The University Of Texas System Diminishing viral gene expression by promoter replacement
US6380394B1 (en) 1996-12-13 2002-04-30 The Scripps Research Institute Epothilone analogs
US6441186B1 (en) 1996-12-13 2002-08-27 The Scripps Research Institute Epothilone analogs
US6660758B1 (en) 1996-12-13 2003-12-09 The Scripps Research Institute Epothilone analogs
US6034072A (en) 1997-02-10 2000-03-07 Genemedicine, Inc. IL-2 gene expression and delivery systems and uses
DE19713213A1 (de) 1997-03-28 1998-10-01 Ruebben Alexander Dr Med Metallstent zur verlängerten Offenhaltung von Hohlorganen
AUPO742497A0 (en) * 1997-06-18 1997-07-10 N.J. Phillips Pty. Limited An applicator
US6605599B1 (en) 1997-07-08 2003-08-12 Bristol-Myers Squibb Company Epothilone derivatives
JP2001512723A (ja) 1997-08-09 2001-08-28 シエーリング アクチエンゲゼルシヤフト 新規エポチロン誘導体、その製法およびその薬学的使用
US6365749B1 (en) 1997-12-04 2002-04-02 Bristol-Myers Squibb Company Process for the preparation of ring-opened epothilone intermediates which are useful for the preparation of epothilone analogs
US6380395B1 (en) 1998-04-21 2002-04-30 Bristol-Myers Squibb Company 12, 13-cyclopropane epothilone derivatives
US6498257B1 (en) 1998-04-21 2002-12-24 Bristol-Myers Squibb Company 2,3-olefinic epothilone derivatives
DE19820599A1 (de) 1998-05-08 1999-11-11 Biotechnolog Forschung Gmbh Epothilonderivate, Verfahren zu deren Herstellung und deren Verwendung
DE19826988A1 (de) 1998-06-18 1999-12-23 Biotechnolog Forschung Gmbh Epothilon-Nebenkomponenten
AU1309900A (en) * 1998-09-29 2000-04-17 University Of Southern California Contortrostatin (cn) and methods for its use in preventing metastasis and other conditions
DE19848306A1 (de) 1998-10-14 2000-04-20 Schering Ag Verfahren zur Herstellung von Epothilon B und Derivaten sowie Zwischenprodukte für dieses Verfahren
US6440944B2 (en) 1998-10-16 2002-08-27 Genvec, Inc. Methods of administering adenoviral vectors
WO2000031247A2 (en) 1998-11-20 2000-06-02 Kosan Biosciences, Inc. Recombinant methods and materials for producing epothilone and epothilone derivatives
DE69910831T2 (de) 1998-12-22 2004-07-15 Novartis Ag Epothilonderivate und ihre verwendung als antitumormittel
US6780620B1 (en) 1998-12-23 2004-08-24 Bristol-Myers Squibb Company Microbial transformation method for the preparation of an epothilone
US6596875B2 (en) 2000-02-07 2003-07-22 James David White Method for synthesizing epothilones and epothilone analogs
EP1161430A2 (de) 1999-02-11 2001-12-12 Schering Aktiengesellschaft Epothilon-derivate, verfahren zu deren herstellung und ihre pharmazeutische verwendung
US6406722B1 (en) 1999-02-18 2002-06-18 Robert G. Gallaher Method of treating viral infections and lesions with taxane compounds
NZ513268A (en) 1999-02-18 2004-05-28 Schering Ag 16-halogen-epothilone derivatives, method for producing them and their pharmaceutical use
US6387664B1 (en) * 1999-02-26 2002-05-14 Secretary Of Agency Of Industrial Science And Technology Sparc fusion protein and method for producing the same
JP3012931B1 (ja) * 1999-02-26 2000-02-28 工業技術院長 Ｓｐａｒｃ融合タンパク質およびその製造方法
AU772750C (en) 1999-04-30 2005-02-24 Schering Aktiengesellschaft 6-alkenyl-, 6-alkinyl- and 6-epoxy-epothilone derivatives, process for their production, and their use in pharmaceutical preparations
US6878699B1 (en) 1999-05-21 2005-04-12 University Of Hawaii Taccalonolide microtubule stabilizing agents
US20050042275A1 (en) 1999-08-04 2005-02-24 Jean-Claude Sonntag Epothilone compositions
US6294374B1 (en) 1999-10-08 2001-09-25 The Scripps Research Institute Use of catalytic antibodies for synthesizing epothilone
JP2004500357A (ja) * 1999-12-10 2004-01-08 ザ・ユニバーシティー・オブ・サザン・カリフォルニア コントートロスタチン（ｃｎ）並びに転移及びその他の症状の予防におけるその使用法
US6518421B1 (en) 2000-03-20 2003-02-11 Bristol-Myers Squibb Company Process for the preparation of epothilone analogs
US6593115B2 (en) 2000-03-24 2003-07-15 Bristol-Myers Squibb Co. Preparation of epothilone intermediates
TWI310684B (en) 2000-03-27 2009-06-11 Bristol Myers Squibb Co Synergistic pharmaceutical kits for treating cancer
DE10020517A1 (de) 2000-04-19 2001-10-25 Schering Ag Neue Epothilon-Derivate, Verfahren zu deren Herstellung und ihre pharmazeutische Verwendung
US6489314B1 (en) 2001-04-03 2002-12-03 Kosan Biosciences, Inc. Epothilone derivatives and methods for making and using the same
US6589968B2 (en) 2001-02-13 2003-07-08 Kosan Biosciences, Inc. Epothilone compounds and methods for making and using the same
US6998256B2 (en) 2000-04-28 2006-02-14 Kosan Biosciences, Inc. Methods of obtaining epothilone D using crystallization and /or by the culture of cells in the presence of methyl oleate
WO2001092255A2 (en) 2000-05-26 2001-12-06 Kosan Biosciences, Inc. Epothilone derivatives and methods for making and using the same
US6638742B1 (en) 2000-07-07 2003-10-28 University Of Portland Methods for obtaining taxanes
UA75365C2 (en) 2000-08-16 2006-04-17 Bristol Myers Squibb Co Epothilone analog polymorph modifications, a method for obtaining thereof (variants), a pharmaceutical composition based thereon
WO2002032844A2 (de) 2000-10-16 2002-04-25 Morphochem Ag Epothilone-synthesebausteine iii und iv: unsymmetrisch substituierte acyloine und acyloinderivate, verfahren zu deren herstellung sowie verfahren zur herstellung von epothilon b, d und epothilonderivaten
JP2004514433A (ja) 2000-11-22 2004-05-20 ノバルティス　アクチエンゲゼルシャフト エポチロン耐性セルライン
CA2436326C (en) 2001-01-09 2012-08-14 Merck Patent Gesellschaft Mit Beschraenkter Haftung Combination therapy using receptor tyrosine kinase inhibitors and angiogenesis inhibitors
KR100851719B1 (ko) 2001-01-25 2008-08-11 브리스톨-마이어스스퀴브컴파니 암 치료용 에포틸론 유사체의 투여 방법
JP2004521122A (ja) 2001-01-25 2004-07-15 ブリストル−マイヤーズ　スクイブ　カンパニー エポチロン類似体の非経口製剤
US20030004338A1 (en) 2001-02-01 2003-01-02 Li Wen Sen Process for the preparation of epothilone analogs
US6893859B2 (en) 2001-02-13 2005-05-17 Kosan Biosciences, Inc. Epothilone derivatives and methods for making and using the same
IL156988A0 (en) 2001-02-20 2004-02-08 Bristol Myers Squibb Co Pharmaceutical compositions containing epothilone derivatives
EP1368030A1 (en) 2001-02-20 2003-12-10 Bristol-Myers Squibb Company Epothilone derivatives for the treatment of refractory tumors
DE60232719D1 (de) 2001-02-27 2009-08-06 Novartis Ag Kombination enthaltend einen inhibitor der signaltransduktion und ein epothilonderivat
SK11082003A3 (sk) 2001-03-14 2004-08-03 Bristol-Myers Squibb Company Kombinácia analógov epotilónu a chemoterapeutických činidiel na liečenie proliferatívnych ochorení
CN100540001C (zh) 2001-03-19 2009-09-16 诺瓦提斯公司 包含止泻药和埃坡霉素或埃坡霉素衍生物的组合
US6906188B2 (en) 2001-04-30 2005-06-14 State Of Oregon Acting By And Through The State Board Of Higher Education On Behalf Of Oregon State University Method for synthesizing epothilones and epothilone analogs
US20030023082A1 (en) 2001-05-15 2003-01-30 Gary Ashley Epothilone derivatives and methods for making and using the same
MXPA03010909A (es) 2001-06-01 2004-02-17 Bristol Myers Squibb Co Derivados de epotilona.
DE10138347A1 (de) 2001-08-03 2003-02-27 Schering Ag Geschützte 3,5-Dihydroxy-2,2-dimethyl-valeronitrile für die Synthese von Epothilonen- und Derivaten und Verfahren zur Herstellung
EP1420780B1 (en) 2001-08-23 2008-10-01 Novartis AG Cyclopropyl and cyclobutyl epothilone analogs
US20030186334A1 (en) 2001-09-12 2003-10-02 Temple University - Of The Commonwealth System Of Higher Education KTS-disintegrins
WO2003029195A1 (en) 2001-09-28 2003-04-10 Sumika Fine Chemicals Co., Ltd. Intermediates for epothilone derivative and process for producing these
AU2002363803A1 (en) 2001-11-15 2003-05-26 Kosan Biosciences, Inc. Method for making epothilone compounds by bioconversion with microorganisms
TW200408407A (en) 2001-11-30 2004-06-01 Dana Farber Cancer Inst Inc Methods and compositions for modulating the immune system and uses thereof
DE10164592A1 (de) 2001-12-21 2003-07-03 Schering Ag C1-C6-Epothilon-Fragmente und Verfahren für die Herstellung von C1-C6-Fragmenten von Epothilonen und deren Derivaten
TW200303202A (en) 2002-02-15 2003-09-01 Bristol Myers Squibb Co Method of preparation of 21-amino epothilone derivatives
WO2003074521A1 (en) 2002-03-01 2003-09-12 University Of Notre Dame Derivatives of epothilone b and d and synthesis thereof
ATE452896T1 (de) 2002-03-12 2010-01-15 Bristol Myers Squibb Co C3-cyanoepothilonderivate
AU2003218107A1 (en) 2002-03-12 2003-09-29 Bristol-Myers Squibb Company C12-cyano epothilone derivatives
RU2358730C2 (ru) 2002-05-01 2009-06-20 Новартис Аг Производное эпотилона для лечения гепатомы и других раковых заболеваний
TW200400191A (en) 2002-05-15 2004-01-01 Bristol Myers Squibb Co Pharmaceutical compositions and methods of using C-21 modified epothilone derivatives
KR20050043796A (ko) 2002-05-20 2005-05-11 코산 바이오사이언시즈, 인코포레이티드 에포틸론 ｄ의 투여방법
US7799561B2 (en) 2002-06-12 2010-09-21 Sigma-Aldrich, Co. Affinity peptides and method for purification of recombinant proteins
AU2003243561A1 (en) 2002-06-14 2003-12-31 Bristol-Myers Squibb Company Combination of epothilone analogs and chemotherapeutic agents for the treatment of proliferative diseases
CN100439374C (zh) 2002-08-02 2008-12-03 诺瓦提斯公司 埃坡霉素衍生物
US7053201B2 (en) 2002-08-30 2006-05-30 National Defense Medical Center Nucleic acid molecules and polypeptides related to h-ADAM7
TWI291464B (en) 2002-09-23 2007-12-21 Bristol Myers Squibb Co Methods for the preparation, isolation and purification of epothilone B, and X-ray crystal structures of epothilone B
GB0230024D0 (en) 2002-12-23 2003-01-29 Novartis Ag Organic compounds
JP2004217535A (ja) 2003-01-10 2004-08-05 Nec Soft Ltd 蛋白質ｔｒｉｍｅｓｔａｔｉｎの結晶化、構造座標の決定、構造座標の使用
US7763430B2 (en) * 2003-04-22 2010-07-27 Baxter International Inc. Diagnostic assay for anti-von Willebrand Factor cleaving protease (ADAMTS13) antibodies
EP1785416A3 (en) 2003-09-25 2007-05-30 Tapestry Pharmaceuticals, Inc. 9, 10-alpha, alpha-OH-Taxane Analogs and methods for production thereof
JP5616572B2 (ja) 2004-12-17 2014-10-29 モナッシュ ユニバーシティ 哺乳類修飾ａｄａｍ１０プロテアーゼまたはそのフラグメント、単離核酸、遺伝子構築物、宿主細胞、抗体、及び産生方法
CA2597647A1 (en) 2005-02-11 2007-08-02 University Of Southern California Method of expressing proteins with disulfide bridges
WO2007030743A2 (en) 2005-09-08 2007-03-15 Massachusetts Eye & Ear Infirmary Cochlear implants containing biological cells and uses thereof
EP2029156A4 (en) 2006-05-01 2010-07-21 Univ Southern California COMBINATION THERAPY FOR CANCER TREATMENT
WO2008143733A2 (en) 2007-03-02 2008-11-27 Dohney Eye Institute Biocompatible implants and methods of making and attaching the same
US8802394B2 (en) 2008-11-13 2014-08-12 Radu O. Minea Method of expressing proteins with disulfide bridges with enhanced yields and activity
US20120142603A1 (en) 2009-02-12 2012-06-07 University Of Southern California Bioadhesive patch for sutureless closure of soft tissue
EP2534171A4 (en) 2010-02-11 2013-07-17 Univ Southern California MODIFIED ADAM DISINTEGRIN DOMAIN POLYPEPTIDES AND USES THEREOF

Non-Patent Citations (2)

* Cited by examiner, † Cited by third party
Title
None
See also references of EP1856255A4

Cited By (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN108864291A (zh) * 2011-11-23 2018-11-23 拜奥文斯瑞有限公司 重组蛋白及其治疗用途
EP3505532A4 (en) * 2016-08-25 2020-04-22 Nexgen Biotechnologies, Inc. SCORPION POISON FUSION PROTEIN WITH IMPROVED EFFECT IN THE PROLIFERATION OF SKIN CELLS AND COSMETIC COMPOSITION, THEREFORE AS AN ACTIVE SUBSTANCE TO REDUCE SKIN WRINKLES, TO IMPROVE THE SKIN ELASTICITY AND TO PREVENT THE AGE
US10745451B2 (en) 2016-08-25 2020-08-18 Nexgen Biotechnologies, Inc. Scorpion toxin fusion protein with enhanced skin cell proliferation effect and cosmetic composition for anti-wrinkle, enhancing skin elasticity and anti-aging comprising the same as an effective ingredient

Also Published As

Publication number Publication date
AU2006336468B2 (en) 2012-04-12
US20110097388A1 (en) 2011-04-28
US8110542B2 (en) 2012-02-07
US20130345399A1 (en) 2013-12-26
US7754850B2 (en) 2010-07-13
US20060246541A1 (en) 2006-11-02
AU2006336468A1 (en) 2007-08-02
JP2008536479A (ja) 2008-09-11
EP1856255A4 (en) 2010-01-27
US20120301453A1 (en) 2012-11-29
WO2007086879A3 (en) 2009-06-11
EP2634252A2 (en) 2013-09-04
US8685668B2 (en) 2014-04-01
CA2597647A1 (en) 2007-08-02
EP2634252B1 (en) 2018-12-19
CN101535492A (zh) 2009-09-16
EP2634252A3 (en) 2013-11-13
EP1856255A2 (en) 2007-11-21
AU2006336468A2 (en) 2010-04-29
US8338365B2 (en) 2012-12-25

Similar Documents

Publication Publication Date Title
US8338365B2 (en) Inhibiting integrin receptor binding with non-native monomeric disintegrin or monomeric disintegrin domains
WO1998056930A9 (en) Methods for producing heterologous disulfide bond-containing polypeptides in bacterial cells
Minea et al. Development of a novel recombinant disintegrin, contortrostatin, as an effective anti-tumor and anti-angiogenic agent
US8802394B2 (en) Method of expressing proteins with disulfide bridges with enhanced yields and activity
EP1054063B2 (en) Process for the production of naturally folded and secreted proteins
HK1189033A (en) Method of expressing proteins with disulfide bridges
HK1189033B (en) Method of expressing proteins with disulfide bridges
AU2002221815B2 (en) Methods for large scale production of recombinant DNA-derived tPA or K2S molecules
JP4663524B2 (ja) ＯｍｐＴプロテアーゼ変異体を用いたポリペプチドの切断方法
Swartz et al. Methods for producing heterologous disulfide bond-containing polypeptides in bacterial cells
AU2002221815A1 (en) Methods for large scale production of recombinant DNA-derived tPA or K2S molecules
Arredondo et al. The problem of expression of multidisulfide bonded recombinant proteins in E. coli
WO2008065673A1 (en) A method for producing n-terminal methioine free polypeptides in microbial host cells
Bonnecaze et al. Laura Segatori
WO2007127589A2 (en) Artificial disulfide isomerases and uses thereof

Legal Events

Date Code Title Description
WWE Wipo information: entry into national phase

Ref document number: 200680011760.6

Country of ref document: CN

WWE Wipo information: entry into national phase

Ref document number: 2007556197

Country of ref document: JP

ENP Entry into the national phase

Ref document number: 2597647

Country of ref document: CA

NENP Non-entry into the national phase

Ref country code: DE

WWE Wipo information: entry into national phase

Ref document number: 2006336468

Country of ref document: AU

Ref document number: 2006849695

Country of ref document: EP

ENP Entry into the national phase

Ref document number: 2006336468

Country of ref document: AU

Date of ref document: 20060209

Kind code of ref document: A

121 Ep: the epo has been informed by wipo that ep was designated in this application