Abstract: The invention discloses a deuterated camptothecin derivative and its antibody-drug conjugate (ADC), and combines the deuteration technology with camptothecin ADC to discover improved deuterated camptothecin ADC drug, so that it has higher safety and efficacy and can better meet the clinical challenge.

Abstract: A method of preventing, reducing a risk of, or treating a virus infection, or preventing or treating a symptom caused by the virus in a subject, said method comprising administering to said subject an effective amount of a fusion protein, wherein the fusion protein comprises a variant angiotensin converting enzyme 2 (ACE2) domain covalently fused to a Fc domain. The variant ACE2 domain comprises a N-terminal deletion, a C-terminal deletion, or both, relative to a full-length wildtype ACE2 having a SEQ ID NO. 1, and the variant ACE2 domain has ACE2 activity. The virus may be SARS-CoV, SARS-CoV-2, or MERS-CoV. The symptom comprises Severe Acute Respiratory Syndrome (SARS), Middle East Respiratory Syndrome (MERS), Acute Respiratory Distress Syndrome (ARDS), Pulmonary Arterial Hypertension (PAH), or Coronavirus Disease 2019 (COVID-19).

Abstract: A fusion protein, comprising a variant angiotensin converting enzyme 2 (ACE2) domain covalently fused to a Fc domain. The variant ACE2 domain has a N-terminal deletion, a C-terminal deletion, or both, relative to a full-length wildtype ACE2 having a SEQ ID NO: 1. The variant ACE2 domain has ACE2 activity.

Abstract: The present disclosure relates to antibodies, in particular monoclonal antibodies of murine, chimeric, and humanized origin, that specifically bind to the human TROP2 protein, and to the amino acid and nucleotide sequences encoding these antibodies. The disclosure also discloses the use of these antibodies as a diagnostic reagent or a drug in the diagnostic and/or therapeutic management of malignancies or any lesion related to the overexpression of said receptor.

Abstract: A camptothecin drug having a highly stable hydrophilic connecting unit and its conjugate, or its pharmaceutically acceptable salt thereof, including methods for preparation thereof, and its applications in preventing and/or treating cancer. The conjugate can specifically bind to receptors highly expressed in tumor cells. The conjugates have excellent water solubility, stability, and homogeneity, and can be used for preventing and/or treating tumors and/or other diseases.

Abstract: An antitumor pharmaceutical camptothecin derivative and an antibody-drug conjugate thereof. By means of a series of molecular structure modifications, an optimal camptothecin antitumor drug is obtained, so as to be more suitable as a drug for antibody conjugation.

Abstract: The present application discloses a camptothecin drug and its antibody conjugate. Based on a comprehensive understanding of ADC drugs, the inventor designed a series of active anti-tumor exatecan-derivatives. The designed anti-tumor molecular compound showed good anti-tumor activity in the experiment.

Abstract: By inserting cysteine (C) into a heavy chain and/or a light chain of a target antibody at specific insertion site, and performing a site-specific conjugation through a free thiol group (—SH) from the site-specific inserted cysteine and a linker conjugated with a highly potent small molecule cytotoxin, a cysteine modified antibody-drug conjugate with good homogeneity is provided. The specific insertion sites of cysteine are position 205 and/or position 206 (Kabat numbering scheme) of the light chain of the antibody, and/or position 439 (Kabat numbering scheme) of the heavy chain.

Abstract: Disclosed in the present invention is a cysteine-modified antibody-toxin conjugate. The cysteine-modified antibody-toxin conjugate is characterized in that: the antibody is an antibody in which cysteine is inserted on a fixed point, and insertion sites of the cysteine comprising one or more of the following sites: a 110th site, a IIIth site and a 142th site of a light chain in a Kappa/?L light chain constant region, and a 254th site, a 255th site, a 258th, a 259th site, a 354th site, a 355th site, a 357th site, a 378th site, a 379th site, a 386th site, a 387th site or a 410th site of a heavy chain of a heavy chain constant region of an IgG antibody.

Abstract: A bispecific tetravalent antibody comprising an IgG having a pair of heavy chains and a pair of light chains, and two scFv components being connected to either C or N terminals of the heavy or light chains. The bispecific tetravalent antibody may have a binding specificity for two different members of EGFR family.

Abstract: A bicyclic octapeptide derivative is conjugated to a corresponding target-binding group by a special chemical structure. The structure of the derivative is stable in blood plasma and decomposes into a drug as an active ingredient in a specific biological environment, thereby maximizing killing effect on target cells and minimizing toxic side effects on non-target cells. The derivative can be used in the treatment of various malignant tumors.

Abstract: The present invention provides a special drug conjugate having a hydrophilic acidic stabilization junction. Compared with a conjugate having a lower drug loading, due to the introduction of the acidic stabilization junction, the conjugate in the present invention can also have a higher drug loading (that is, each targeted reagent has more hydrophilic drug junctions), keeps a desired PK property and has a same or better activity in a body.

Abstract: A bispecific tetravalent antibody comprising an IgG having a pair of heavy chains and a pair of light chains, and two scFv components being connected to either C or N terminals of the heavy or light chains. The bispecific tetravalent antibody may have a binding specificity for two different members of EGFR family.

Abstract: Disclosed is a non-natural amatoxin-type antibody conjugate, said conjugate similar to the natural amatoxin is linked to a biopharmaceutically acceptable salt with a target biomolecule so as to obtain stability in blood plasma, and efficiently kill tumor cells in cells.

Abstract: By inserting cysteine (C) into a heavy chain and/or a light chain of a target antibody at specific insertion site, and performing a site-specific conjugation through a free thiol group (—SH) from the site-specific inserted cysteine and a linker conjugated with a highly potent small molecule cytotoxin, a cysteine modified antibody-drug conjugate with good homogeneity is provided.

Abstract: A bispecific tetravalent antibody comprising an IgG having a pair of heavy chains and a pair of light chains, and two scFv components being connected to either C or N terminals of the heavy or light chains. The bispecific tetravalent antibody may have a binding specificity for two different members of EGFR family.