[go: up one dir, main page]

Ohri et al., 2018 - Google Patents

High-throughput cysteine scanning to identify stable antibody conjugation sites for maleimide-and disulfide-based linkers

Ohri et al., 2018

View PDF
Document ID
9595953711436825374
Author
Ohri R
Bhakta S
Fourie-O’Donohue A
dela Cruz-Chuh J
Tsai S
Cook R
Wei B
Ng C
Wong A
Bos A
Farahi F
Bhakta J
Pillow T
Raab H
Vandlen R
Polakis P
Liu Y
Erickson H
Junutula J
Kozak K
Publication year
Publication venue
Bioconjugate Chemistry

External Links

Snippet

THIOMAB antibody technology utilizes cysteine residues engineered onto an antibody to allow for site-specific conjugation. The technology has enabled the exploration of different attachment sites on the antibody in combination with small molecules, peptides, or proteins …
Continue reading at www.academia.edu (PDF) (other versions)

Classifications

    • AHUMAN NECESSITIES
    • A61MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61KPREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K47/00Medicinal preparations characterised by the non-active ingredients used, e.g. carriers, inert additives
    • A61K47/48Medicinal preparations characterised by the non-active ingredients used, e.g. carriers, inert additives the non-active ingredient being chemically bound to the active ingredient, e.g. polymer drug conjugates
    • A61K47/48369Medicinal preparations characterised by the non-active ingredients used, e.g. carriers, inert additives the non-active ingredient being chemically bound to the active ingredient, e.g. polymer drug conjugates the modifying part being an antibody, an immunoglobulin, or a fragment thereof, e.g. a Fc-fragment
    • A61K47/48507Medicinal preparations characterised by the non-active ingredients used, e.g. carriers, inert additives the non-active ingredient being chemically bound to the active ingredient, e.g. polymer drug conjugates the modifying part being an antibody, an immunoglobulin, or a fragment thereof, e.g. a Fc-fragment the modifying agent being a well defined antibody or immunoglobulin bearing at least one antigen-binding site
    • A61K47/48515Medicinal preparations characterised by the non-active ingredients used, e.g. carriers, inert additives the non-active ingredient being chemically bound to the active ingredient, e.g. polymer drug conjugates the modifying part being an antibody, an immunoglobulin, or a fragment thereof, e.g. a Fc-fragment the modifying agent being a well defined antibody or immunoglobulin bearing at least one antigen-binding site not used; see subgroups
    • AHUMAN NECESSITIES
    • A61MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61KPREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K47/00Medicinal preparations characterised by the non-active ingredients used, e.g. carriers, inert additives
    • A61K47/48Medicinal preparations characterised by the non-active ingredients used, e.g. carriers, inert additives the non-active ingredient being chemically bound to the active ingredient, e.g. polymer drug conjugates
    • A61K47/48369Medicinal preparations characterised by the non-active ingredients used, e.g. carriers, inert additives the non-active ingredient being chemically bound to the active ingredient, e.g. polymer drug conjugates the modifying part being an antibody, an immunoglobulin, or a fragment thereof, e.g. a Fc-fragment
    • A61K47/48376Medicinal preparations characterised by the non-active ingredients used, e.g. carriers, inert additives the non-active ingredient being chemically bound to the active ingredient, e.g. polymer drug conjugates the modifying part being an antibody, an immunoglobulin, or a fragment thereof, e.g. a Fc-fragment drug-antibody or immunoglobulin conjugates defined by the pharmacologically or therapeutically active agent
    • A61K47/48384Medicinal preparations characterised by the non-active ingredients used, e.g. carriers, inert additives the non-active ingredient being chemically bound to the active ingredient, e.g. polymer drug conjugates the modifying part being an antibody, an immunoglobulin, or a fragment thereof, e.g. a Fc-fragment drug-antibody or immunoglobulin conjugates defined by the pharmacologically or therapeutically active agent drug conjugated to an antibody or immunoglobulin, e.g. cisplatin-antibody conjugates
    • AHUMAN NECESSITIES
    • A61MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61KPREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K47/00Medicinal preparations characterised by the non-active ingredients used, e.g. carriers, inert additives
    • A61K47/48Medicinal preparations characterised by the non-active ingredients used, e.g. carriers, inert additives the non-active ingredient being chemically bound to the active ingredient, e.g. polymer drug conjugates
    • A61K47/48169Medicinal preparations characterised by the non-active ingredients used, e.g. carriers, inert additives the non-active ingredient being chemically bound to the active ingredient, e.g. polymer drug conjugates the modifying agent being an organic macromolecular compound, i.e. an oligomeric, polymeric, dendrimeric molecule
    • A61K47/48192Medicinal preparations characterised by the non-active ingredients used, e.g. carriers, inert additives the non-active ingredient being chemically bound to the active ingredient, e.g. polymer drug conjugates the modifying agent being an organic macromolecular compound, i.e. an oligomeric, polymeric, dendrimeric molecule the organic macromolecular compound has been obtained otherwise than by reactions only involving carbon-to-carbon unsaturated bonds, e.g. polyureas, polyurethanes
    • A61K47/48215Medicinal preparations characterised by the non-active ingredients used, e.g. carriers, inert additives the non-active ingredient being chemically bound to the active ingredient, e.g. polymer drug conjugates the modifying agent being an organic macromolecular compound, i.e. an oligomeric, polymeric, dendrimeric molecule the organic macromolecular compound has been obtained otherwise than by reactions only involving carbon-to-carbon unsaturated bonds, e.g. polyureas, polyurethanes the organic macromolecular compound being a polyoxyalkylene oligomer, polymer, dendrimer, e.g. PEG, PPG, PEO, polyglycerol
    • AHUMAN NECESSITIES
    • A61MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61KPREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K47/00Medicinal preparations characterised by the non-active ingredients used, e.g. carriers, inert additives
    • A61K47/48Medicinal preparations characterised by the non-active ingredients used, e.g. carriers, inert additives the non-active ingredient being chemically bound to the active ingredient, e.g. polymer drug conjugates
    • A61K47/48007Medicinal preparations characterised by the non-active ingredients used, e.g. carriers, inert additives the non-active ingredient being chemically bound to the active ingredient, e.g. polymer drug conjugates the pharmacologically- or therapeutically-active agent being covalently bound or complexed to a modifying agent
    • A61K47/48023Medicinal preparations characterised by the non-active ingredients used, e.g. carriers, inert additives the non-active ingredient being chemically bound to the active ingredient, e.g. polymer drug conjugates the pharmacologically- or therapeutically-active agent being covalently bound or complexed to a modifying agent the modifying agent being an organic compound
    • A61K47/48061Medicinal preparations characterised by the non-active ingredients used, e.g. carriers, inert additives the non-active ingredient being chemically bound to the active ingredient, e.g. polymer drug conjugates the pharmacologically- or therapeutically-active agent being covalently bound or complexed to a modifying agent the modifying agent being an organic compound the modifying agent being a heterocyclic compound
    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/53Immunoassay; Biospecific binding assay
    • AHUMAN NECESSITIES
    • A61MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61KPREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K47/00Medicinal preparations characterised by the non-active ingredients used, e.g. carriers, inert additives
    • A61K47/48Medicinal preparations characterised by the non-active ingredients used, e.g. carriers, inert additives the non-active ingredient being chemically bound to the active ingredient, e.g. polymer drug conjugates
    • A61K47/48238Medicinal preparations characterised by the non-active ingredients used, e.g. carriers, inert additives the non-active ingredient being chemically bound to the active ingredient, e.g. polymer drug conjugates the modifying agent being a protein, peptide, polyamino acid

Similar Documents

Publication Publication Date Title
Ohri et al. High-throughput cysteine scanning to identify stable antibody conjugation sites for maleimide-and disulfide-based linkers
Patterson et al. Improving the serum stability of site-specific antibody conjugates with sulfone linkers
Su et al. Modulating antibody–drug conjugate payload metabolism by conjugation site and linker modification
Puthenveetil et al. Development of solid-phase site-specific conjugation and its application toward generation of dual labeled antibody and fab drug conjugates
Su et al. Custom-designed affinity capture LC-MS F (ab′) 2 assay for biotransformation assessment of site-specific antibody drug conjugates
Li et al. Site-specific dual antibody conjugation via engineered cysteine and selenocysteine residues
Lhospice et al. Site-specific conjugation of monomethyl auristatin E to anti-CD30 antibodies improves their pharmacokinetics and therapeutic index in rodent models
Vollmar et al. Attachment site cysteine thiol p K a is a key driver for site-dependent stability of THIOMAB antibody–drug conjugates
Dennler et al. Transglutaminase-based chemo-enzymatic conjugation approach yields homogeneous antibody–drug conjugates
Pillow et al. Site-specific trastuzumab maytansinoid antibody–drug conjugates with improved therapeutic activity through linker and antibody engineering
Behrens et al. Antibody–drug conjugates (ADCs) derived from interchain cysteine cross-linking demonstrate improved homogeneity and other pharmacological properties over conventional heterogeneous ADCs
Wakankar et al. Physicochemical stability of the antibody− drug conjugate trastuzumab-DM1: changes due to modification and conjugation processes
Shinmi et al. One-step conjugation method for site-specific antibody–drug conjugates through reactive cysteine-engineered antibodies
Badescu et al. Bridging disulfides for stable and defined antibody drug conjugates
Ponte et al. Understanding how the stability of the thiol-maleimide linkage impacts the pharmacokinetics of lysine-linked antibody–maytansinoid conjugates
He et al. High-resolution accurate-mass mass spectrometry enabling in-depth characterization of in vivo biotransformations for intact antibody-drug conjugates
Guo et al. Characterization and higher-order structure assessment of an interchain cysteine-based ADC: impact of drug loading and distribution on the mechanism of aggregation
Hengel et al. Measurement of in vivo drug load distribution of cysteine-linked antibody–drug conjugates using microscale liquid chromatography mass spectrometry
Le et al. Profiling antibody drug conjugate positional isomers: a system-of-equations approach
Stephan et al. Anti-CD22-MCC-DM1 and MC-MMAF conjugates: impact of assay format on pharmacokinetic parameters determination
Cumnock et al. Trisulfide modification impacts the reduction step in antibody–drug conjugation process
Bahou et al. Disulfide modified IgG1: an investigation of biophysical profile and clinically relevant Fc interactions
Yoder et al. A case study comparing heterogeneous lysine-and site-specific cysteine-conjugated maytansinoid antibody-drug conjugates (ADCs) illustrates the benefits of lysine conjugation
Thompson et al. Straightforward glycoengineering approach to site-specific antibody–pyrrolobenzodiazepine conjugates
Rago et al. Quantitative conjugated payload measurement using enzymatic release of antibody–drug conjugate with cleavable linker