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  • A61K47/6801—Drug-antibody or immunoglobulin conjugates defined by the pharmacologically or therapeutically active agent
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  • A61K47/6801—Drug-antibody or immunoglobulin conjugates defined by the pharmacologically or therapeutically active agent
  • A61K47/6803—Drugs conjugated to an antibody or immunoglobulin, e.g. cisplatin-antibody conjugates
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  • A61K47/6851—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an antibody, an immunoglobulin or a fragment thereof, e.g. an Fc-fragment the modifying agent being an antibody or an immunoglobulin bearing at least one antigen-binding site the antibody targeting a determinant of a tumour cell
• • A—HUMAN NECESSITIES
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  • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
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  • A61K47/50—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates
  • A61K47/51—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent
  • A61K47/68—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an antibody, an immunoglobulin or a fragment thereof, e.g. an Fc-fragment
  • A61K47/6889—Conjugates wherein the antibody being the modifying agent and wherein the linker, binder or spacer confers particular properties to the conjugates, e.g. peptidic enzyme-labile linkers or acid-labile linkers, providing for an acid-labile immuno conjugate wherein the drug may be released from its antibody conjugated part in an acidic, e.g. tumoural or environment
• • A—HUMAN NECESSITIES
  • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
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  • A61P35/00—Antineoplastic agents
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  • C07—ORGANIC CHEMISTRY
  • C07K—PEPTIDES
  • C07K16/00—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies
  • C07K16/18—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from animals or humans
  • C07K16/28—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
  • C07K16/2803—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the immunoglobulin superfamily
• • 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
  • G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
  • G01N33/543—Immunoassay; Biospecific binding assay; Materials therefor with an insoluble carrier for immobilising immunochemicals
• • C—CHEMISTRY; METALLURGY
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  • C07K2317/00—Immunoglobulins specific features
  • C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
  • C07K2317/33—Crossreactivity, e.g. for species or epitope, or lack of said crossreactivity
• • C—CHEMISTRY; METALLURGY
  • C07—ORGANIC CHEMISTRY
  • C07K—PEPTIDES
  • C07K2317/00—Immunoglobulins specific features
  • C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
  • C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
  • C07K2317/565—Complementarity determining region [CDR]
• • C—CHEMISTRY; METALLURGY
  • C07—ORGANIC CHEMISTRY
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  • C07K2317/00—Immunoglobulins specific features
  • C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
  • C07K2317/73—Inducing cell death, e.g. apoptosis, necrosis or inhibition of cell proliferation
• • C—CHEMISTRY; METALLURGY
  • C07—ORGANIC CHEMISTRY
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  • C07K2317/00—Immunoglobulins specific features
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  • C07K2317/77—Internalization into the cell
• • C—CHEMISTRY; METALLURGY
  • C07—ORGANIC CHEMISTRY
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  • C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
  • C07K2317/92—Affinity (KD), association rate (Ka), dissociation rate (Kd) or EC50 value

Definitions

• ROR1 The expression of ROR1 was not detected in most normal tissues, including the heart, spleen, lung and liver, these important human organs, and only a certain expression was detected in the parathyroid gland, pancreatic islets and gastrointestinal tract tissues. In view of the huge difference in the expression of ROR1 in normal tissues and tumor tissues, and in various tumors (including hematological tumors and solid tumors), it can be used as an ideal target for ADC molecular development.
• the light chain variable region comprises LCDR1, LCDR2 and LCDR3 shown in SEQ ID NO: 7, SEQ ID NO: 8 and SEQ ID NO: 9, respectively;
• the present disclosure also provides an immunoconjugate or a pharmaceutically acceptable salt thereof, comprising the anti-ROR1 antibody and an effector molecule as described in any one of the preceding items, wherein the effector molecule is coupled to The anti-ROR1 antibody.
• the effector molecules are selected from radioisotopes, antineoplastic agents, immunomodulators, biological response modifiers, lectins, cytotoxic drugs, chromophores, fluorophores, chemiluminescent compounds, enzymes, metal ions, and the like any combination.
• n is an integer or a decimal of 1 to 10; n is preferably an integer or a decimal of 1 to 8;
• the aforementioned immunoconjugate or a pharmaceutically acceptable salt thereof, wherein the structure of the immunoconjugate is as follows:
• L 1 is selected from -(succinimide-3-yl-N)-WC(O)-, -CH 2 -C(O)-NR 1 -WC(O)- or -C(O)-WC( O)-, wherein W is selected from C 1-8 alkyl or C 1-6 alkyl-cycloalkyl;
• the immunoconjugate or the pharmaceutically acceptable salt thereof according to any one of the preceding items, wherein said L 4 is -NR 3 (CR 4 R 5 )t-, wherein, R 3 , R 4 or R 5 are the same or different, and are each independently a hydrogen atom or a C 1-6 alkyl group, and t is 1 or 2.
• the immunoconjugate or a pharmaceutically acceptable salt thereof according to any one of the preceding items, wherein said L 4 is a PAB group.
• the term "heavy chain” includes the variable region domain VH and the three constant region domains CH1, CH2 and CH3.
• the VH is amino-terminal to the heavy chain, and the CH domain is carboxy-terminal, with CH3 closest to the carboxy-terminus of the polypeptide.
• the heavy chain can be of any isotype, including IgG (including IgGl, IgG2, IgG3, and IgG4 subtypes), IgA (including IgAl and IgA2 subtypes), IgM, and IgE.
• the term “specifically binds”, “specifically binds” or “binds” means that an antibody binds to a certain antigen or epitope thereof with a higher affinity than to another antigen or epitope.
• the antibody binds the antigen or its antigen with an equilibrium dissociation constant (KD) of about 1 x 10 -7 M or less (e.g., about 1 x 10 -8 M or less, about 1 x 10 -9 M or less). gauge.
• the antibody binds the antigen with a KD that is 10%, or less (eg, 1%) of the antibody's KD for binding to a non-specific antigen (eg, BSA, casein).
• KD can be measured using methods known in the art, for example by Surface plasmon resonance measurements.
• antibodies that specifically bind to an antigen or an epitope thereof may have cross-reactivity to other related antigens, e.g. , cyno), chimpanzee (Pan troglodytes) (chimpanzee, chimp) or marmoset (Callithrix jacchus) (commonmarmoset, marmoset)) are cross-reactive.
• FcR expression on hematopoietic cells is summarized in Table 3 on page 464 of Ravetch and Kinet, Annu. Rev. Immunol. 9:457-92 (1991).
• an in vitro ADCC assay can be performed, such as those described in US Pat. No. 5,500,362 or 5,821,337.
• Useful effector cells for such assays include peripheral blood mononuclear cells (PBMC) and natural killer (NK) cells.
• PBMC peripheral blood mononuclear cells
• NK natural killer
• ADCC activity of an antibody of interest can also be assessed in vivo, eg, in an animal model such as that disclosed in Clynes et al., (USA) 95:652-656 (1998).
• ADCP antibody-dependent cellular phagocytosis
• complement-dependent cytotoxicity refers to a cell death-inducing mechanism in which the Fc effector domain of a target-binding antibody binds and activates complement component C1q, which in turn activates the complement cascade, resulting in target cell death.
• Activation of complement can also result in the deposition of complement components on the surface of target cells that promote CDC by binding to complement receptors (eg, CR3) on leukocytes.
• complement receptors eg, CR3
• isolated means free from its naturally occurring state, and in this context means that the specified molecule is substantially free of other biomolecules, such as nucleic acids, proteins, lipids, carbohydrates, or other materials, such as cellular debris and growth medium.
• isolated is not intended to mean the complete absence of these materials or the absence of water, buffers or salts, unless they are present in amounts that significantly interfere with the experimental or therapeutic use of the compounds as described herein.
• Alkyl may be substituted or unsubstituted, and when substituted, it may be substituted at any available point of attachment, substituents are preferably selected from D atoms, halogen, alkoxy, haloalkyl, haloalkoxy, ring One or more of alkyloxy, heterocyclyloxy, hydroxy, hydroxyalkyl, cyano, amino, nitro, cycloalkyl, heterocyclyl, aryl and heteroaryl.
• the term "therapeutically effective amount” refers to a non-toxic but sufficient amount of the drug or agent to achieve the desired effect.
• the determination of the effective amount varies from person to person, depending on the age and general condition of the subject, and also depends on the specific active substance. The appropriate effective amount in each case can be determined by those skilled in the art according to routine tests.
• the pharmaceutical composition can be in the form of a sterile injectable aqueous or oily suspension for intramuscular and subcutaneous administration.
• This suspension may be formulated according to the known art using those suitable dispersing or wetting agents and suspending agents which have been mentioned above.
• the sterile injectable preparation can also be a sterile injectable solution or suspension prepared in a non-toxic parenterally acceptable diluent or solvent, for example a solution in 1,3-butanediol.
• sterile fixed oils are conveniently employed as a solvent or suspending medium.
• any bland fixed oil may be employed including synthetic mono- or diglycerides.
• fatty acids such as oleic acid are prepared as injectables.
• an “effective amount” is generally sufficient to reduce the severity and/or frequency of symptoms, eliminate those symptoms and/or their underlying causes, prevent the occurrence of symptoms and/or their underlying causes, and/or ameliorate or ameliorate the impairment caused by or associated with the disease state (e.g. lung disease).
• the effective amount is a therapeutically or prophylactically effective amount.
• a “therapeutically effective amount” is sufficient to treat a disease state or symptom, especially a state or symptom associated with the disease state, or otherwise prevent, hinder, delay or reverse the disease state or any other adverse effect in any way related to the disease state. The amount of progression of the desired symptoms.
• the anti-ROR1 antibody Ab1 in WO2018237335 is used as a positive control, and its sequences are as follows:
• Compound D1 (Hanxiang Biotechnology, CAS: 646502-53-6, 2.92mg, 2218nmol) was dissolved in 140 ⁇ L DMSO, added to the above reaction solution, placed in a water bath shaker, and shaken at 25°C for 3 hours. Stop responding.
• the reaction solution was desalted and purified with Sephadex G25 gel column (elution phase: 0.05M PBS buffered aqueous solution with pH 6.5, containing 0.001M EDTA), to obtain the PBS buffer solution (2.25mg/mL, 13.5mL), stored in refrigerator at 4°C.
• Embodiment 6 Preparation of ADC-4
• Test Example 4 Cross-binding ability to rat/mouse ROR1 antigen
• Test Example 5 In vivo drug efficacy evaluation of ADC molecule high expression CDX model
• Tumor inhibition rate TGI(%) 1-T/C(%).
• ADC samples were prepared into different concentrations with PBS, and diluted five times with PBS, a total of 8 concentrations. Take out the cell culture plate and add 15 ⁇ L of 10 ⁇ concentration solution to each well. 5% carbon dioxide and cultured at 37°C for 6 days.
• NDG mice were subcutaneously inoculated with JEKO-1 cells (5 ⁇ 10 6 +50% matrigel/200 ⁇ L/mouse) on the right flank, and divided into groups 7 days later, 8 mice/group.
• the average tumor volume of each group was 266.7mm 3 on the day of grouping.
• the ADC compound was administered by intraperitoneal injection at a dose of 2.5mpk/5mpk, administered on the 1st day and 14th day of the grouping respectively, administered twice in total, and observed for 21 days.
• ADC-3-35mpk MTD ⁇ 35mpk (animal died); toxicity manifested as: weight loss, bone marrow suppression, thymus atrophy, liver, lung, kidney and other organ functions were significantly affected.

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