EP1379545A2 - Procede de production de series d'anticorps stables regenerables - Google Patents

Procede de production de series d'anticorps stables regenerables

Info

Publication number
EP1379545A2
EP1379545A2 EP02745239A EP02745239A EP1379545A2 EP 1379545 A2 EP1379545 A2 EP 1379545A2 EP 02745239 A EP02745239 A EP 02745239A EP 02745239 A EP02745239 A EP 02745239A EP 1379545 A2 EP1379545 A2 EP 1379545A2
Authority
EP
European Patent Office
Prior art keywords
antibody
protein
arrays
antibodies
producing stable
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.)
Withdrawn
Application number
EP02745239A
Other languages
German (de)
English (en)
Inventor
Jürgen WEHLAND
Ronald Frank
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.)
Helmholtz Centre for Infection Research
Original Assignee
Helmholtz Centre for Infection Research
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 Helmholtz Centre for Infection Research filed Critical Helmholtz Centre for Infection Research
Publication of EP1379545A2 publication Critical patent/EP1379545A2/fr
Withdrawn legal-status Critical Current

Links

Classifications

    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
    • G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
    • G01N33/6854—Immunoglobulins
    • G01N33/6857—Antibody fragments
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K17/00—Carrier-bound or immobilised peptides; Preparation thereof
    • C07K17/02—Peptides being immobilised on, or in, an organic carrier
    • C07K17/08—Peptides being immobilised on, or in, an organic carrier the carrier being a synthetic polymer
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K17/00—Carrier-bound or immobilised peptides; Preparation thereof
    • C07K17/14—Peptides being immobilised on, or in, an inorganic carrier

Definitions

  • the invention relates to a method for producing stable, regenerable antibody arrays using immobilized antibody binding proteins which can specifically recognize the Fc part of antibodies.
  • Arrays with biological test molecules are also called biochips, particularly in miniaturized form. Proven examples of such arrays are:
  • Nucleic acid arrays from DNA fragments, cDNAs, RNAs, PCR products, plasmids, bacteriophages, synthetic oligonucleotides or synthetic PNA oligomers which are read out by means of hybridization (formation of a double-stranded molecule) on complementary nucleic acid analytes and connecting arrays made of synthetic ones Peptides, their analogs, such as peptoids, oligo-carbamates etc. or generally organic chemical compounds, which are read out by binding to affine protein or other analytes or by enzymatic conversion.
  • Such arrays are currently manufactured according to two different principles by placing the test molecules on already prepared material surfaces: a) by spreading the solution of pre-prepared test compounds once on the surface
  • Previously known chip configurations use either a right-angled x / y arrangement, which is produced with appropriately manufactured photolithography or printing masks, or a circular r ⁇ arrangement, which is generated by a rotational movement of the chip surface (r ⁇ -arrays) and a rapidly clocked metering device becomes. This enables densities of up to 1 million test connections per cm 2 or a few square micrometers per individual surface to be achieved.
  • the invention thus relates to a method for producing stable, regenerable antibody arrays, in which
  • the invention further relates to an antibody array which can be obtained by the method according to the invention, a medical or diagnostic device which has an antibody array according to the invention, and a kit which has an antibody array according to the invention and detection reagents for qualitative or quantitative determination contains bound antigens which have been bound to an antibody array according to the invention.
  • the invention further specifies the use of an antibody array according to the invention or a medical or diagnostic device according to the invention for the qualitative or quantitative determination of antigens.
  • Advantageous and / or preferred embodiments of the invention are the subject of the dependent claims.
  • the planar carrier has a surface made of glass, metal, metal oxides, semimetal oxides or plastic.
  • the antibody binding protein is selected from Fc-specific secondary antibodies, protein A and protein G.
  • the antigen to be determined is a protein.
  • the specific antibodies are "directed” immobilized, i.e. via their Fc part in order not to influence the antigen recognition through the coupling.
  • a grid of proteins that specifically recognize the Fc part of the specific antibodies is covalently bound to the chip surface in question (eg derivatized Fc-specific secondary antibodies or protein A or protein G molecules).
  • Protein / antibody or antibody / antibody complexes are achieved by chemical covalent crosslinking, where be used for common reagents according to the requirements.
  • chemical covalent crosslinking In addition to the stabilization of the protein-protein interactions, there is also an intramolecular stabilization of the specific antibodies, ie a chemical cross-linking of their subunits.
  • Antibody arrays with the highest stability result, which on the one hand prevent dissociation of the special antibodies, eg during storage, and on the other hand also make it possible to treat the antibody arrays under stringent conditions, such as high salt concentrations or low or high pH to prevent non-specific or low affinity interactions with the antibody matrix. This also enables a correspondingly stringent pretreatment of the protein mixtures to be analyzed.
  • the whole process delivers stable and regenerable antibody arrays.

Landscapes

  • Chemical & Material Sciences (AREA)
  • Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Immunology (AREA)
  • Molecular Biology (AREA)
  • Organic Chemistry (AREA)
  • Biochemistry (AREA)
  • Engineering & Computer Science (AREA)
  • General Health & Medical Sciences (AREA)
  • Medicinal Chemistry (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Genetics & Genomics (AREA)
  • Hematology (AREA)
  • Biomedical Technology (AREA)
  • Urology & Nephrology (AREA)
  • Biophysics (AREA)
  • Cell Biology (AREA)
  • Microbiology (AREA)
  • Biotechnology (AREA)
  • Food Science & Technology (AREA)
  • Physics & Mathematics (AREA)
  • Analytical Chemistry (AREA)
  • General Physics & Mathematics (AREA)
  • Pathology (AREA)
  • Inorganic Chemistry (AREA)
  • Peptides Or Proteins (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)

Abstract

L'invention concerne un procédé de production de séries d'anticorps stables, régénérables, caractérisé en ce qu'on utilise des protéines immobilisées liant les anticorps et qui sont capables d'identifier spécifiquement la fraction Fc d'anticorps.
EP02745239A 2001-04-19 2002-04-18 Procede de production de series d'anticorps stables regenerables Withdrawn EP1379545A2 (fr)

Applications Claiming Priority (5)

Application Number Priority Date Filing Date Title
DE10119308 2001-04-19
DE10119308 2001-04-19
DE10162365 2001-12-18
DE10162365 2001-12-18
PCT/EP2002/004311 WO2002085926A2 (fr) 2001-04-19 2002-04-18 Procede de production de series d'anticorps stables regenerables

Publications (1)

Publication Number Publication Date
EP1379545A2 true EP1379545A2 (fr) 2004-01-14

Family

ID=26009128

Family Applications (1)

Application Number Title Priority Date Filing Date
EP02745239A Withdrawn EP1379545A2 (fr) 2001-04-19 2002-04-18 Procede de production de series d'anticorps stables regenerables

Country Status (4)

Country Link
US (1) US20040171068A1 (fr)
EP (1) EP1379545A2 (fr)
JP (1) JP2004536290A (fr)
WO (1) WO2002085926A2 (fr)

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CN104706637A (zh) * 2006-05-18 2015-06-17 卫材R&D管理有限公司 针对甲状腺癌的抗肿瘤剂
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JP5368096B2 (ja) * 2006-08-28 2013-12-18 エーザイ・アール・アンド・ディー・マネジメント株式会社 未分化型胃癌に対する抗腫瘍剤
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CA2704000C (fr) * 2007-11-09 2016-12-13 Eisai R&D Management Co., Ltd. Combinaison d'une substance antiangiogenique et d'un complexe de platine antitumoral
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CA2771403C (fr) 2009-08-19 2015-02-24 Eisai R&D Management Co. Ltd. Composition pharmaceutique contenant un derive de quinoleine
TW201124726A (en) * 2009-10-16 2011-07-16 Univ Texas Compositions and methods for producing coded peptoid libraries
CN102958523B (zh) 2010-06-25 2014-11-19 卫材R&D管理有限公司 使用具有激酶抑制作用的组合的抗肿瘤剂
AU2012246490B2 (en) 2011-04-18 2016-08-04 Eisai R&D Management Co., Ltd. Therapeutic agent for tumor
JP6038128B2 (ja) 2011-06-03 2016-12-07 エーザイ・アール・アンド・ディー・マネジメント株式会社 レンバチニブ化合物に対する甲状腺癌対象及び腎臓癌対象の反応性を予測及び評価するためのバイオマーカー
JPWO2014098176A1 (ja) 2012-12-21 2017-01-12 エーザイ・アール・アンド・ディー・マネジメント株式会社 キノリン誘導体のアモルファス及びその製造方法
CA2912219C (fr) 2013-05-14 2021-11-16 Eisai R&D Management Co., Ltd. Biomarqueurs pour predire et evaluer la reponse de sujets atteints de cancer de l'endometre a des composes a base de lenvatinib
EP3187491A4 (fr) 2014-08-28 2018-08-01 Eisai R&D Management Co., Ltd. Dérivé de quinoline de pureté élevée et son procédé de fabrication
EP3250588A1 (fr) 2015-01-29 2017-12-06 Board of Trustees of Michigan State University Polypeptides cryptiques et leurs utilisations
US20180028662A1 (en) 2015-02-25 2018-02-01 Eisai R&D Management Co., Ltd. Method for Suppressing Bitterness of Quinoline Derivative
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Also Published As

Publication number Publication date
JP2004536290A (ja) 2004-12-02
US20040171068A1 (en) 2004-09-02
WO2002085926A2 (fr) 2002-10-31
WO2002085926A3 (fr) 2003-11-06

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