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Antibody

The Experts below are selected from a list of 261 Experts worldwide ranked by ideXlab platform

Takeshi Imamura – 1st expert on this subject based on the ideXlab platform

  • direct immobilization of gold binding Antibody fragments for immunosensor applications
    Analytical Chemistry, 2010
    Co-Authors: Takahisa Ibii, Masaru Kaieda, Hidenori Shiotsuka, Hideki Watanabe, Mitsuo Umetsu, Izumi Kumagai, Satoru Hatakeyama, Takeshi Imamura

    Abstract:

    A novel method that enables Antibody fragments to be immobilized on a sensor substrate with a high binding capability using molecular recognition has been developed. Using genetic engineering, we fabricated bispecific recombinant Antibody fragments, which consist of two kinds of Antibody fragments: a gold Antibody fragment and a target molecule Antibody fragment. Surface plasmon resonance (SPR) analysis indicated that these gold-binding bispecific Antibody fragments bind directly to the gold substrate with high affinity (KD ∼ 10−9 M). About 70% of the bispecific Antibody fragments immobilized on the gold substrate retained their target protein-binding efficiency. The Sips isotherm was used to assess the heterogeneity in Antibody affinity for the bispecific Antibody fragments. The results showed that the immobilized bispecific Antibody fragments exhibited an increased homogeneity of affinity (KD) to target molecules when compared with monospecific Antibody fragments immobilized by conventional methods. The…

  • Direct immobilization of gold-binding Antibody fragments for immunosensor applications
    Analytical Chemistry, 2010
    Co-Authors: Takahisa Ibii, Masaru Kaieda, Shuichiro Hatakeyama, Hidenori Shiotsuka, Hideki Watanabe, Mitsuo Umetsu, Izumi Kumagai, Takeshi Imamura

    Abstract:

    A novel method that enables Antibody fragments to be immobilized on a sensor substrate with a high binding capability using molecular recognition has been developed. Using genetic engineering, we fabricated bispecific recombinant Antibody fragments, which consist of two kinds of Antibody fragments: a gold Antibody fragment and a target molecule Antibody fragment. Surface plasmon resonance (SPR) analysis indicated that these gold-binding bispecific Antibody fragments bind directly to the gold substrate with high affinity (K(D) approximately 10(-9) M). About 70% of the bispecific Antibody fragments immobilized on the gold substrate retained their target protein-binding efficiency. The Sips isotherm was used to assess the heterogeneity in Antibody affinity for the bispecific Antibody fragments. The results showed that the immobilized bispecific Antibody fragments exhibited an increased homogeneity of affinity (K(D)) to target molecules when compared with monospecific Antibody fragments immobilized by conventional methods. The use of bispecific Antibody fragments to directly immobilize Antibody fragments on a solid-phase substrate offers a useful platform for immunosensor applications.

Takahisa Ibii – 2nd expert on this subject based on the ideXlab platform

  • direct immobilization of gold binding Antibody fragments for immunosensor applications
    Analytical Chemistry, 2010
    Co-Authors: Takahisa Ibii, Masaru Kaieda, Hidenori Shiotsuka, Hideki Watanabe, Mitsuo Umetsu, Izumi Kumagai, Satoru Hatakeyama, Takeshi Imamura

    Abstract:

    A novel method that enables Antibody fragments to be immobilized on a sensor substrate with a high binding capability using molecular recognition has been developed. Using genetic engineering, we fabricated bispecific recombinant Antibody fragments, which consist of two kinds of Antibody fragments: a gold Antibody fragment and a target molecule Antibody fragment. Surface plasmon resonance (SPR) analysis indicated that these gold-binding bispecific Antibody fragments bind directly to the gold substrate with high affinity (KD ∼ 10−9 M). About 70% of the bispecific Antibody fragments immobilized on the gold substrate retained their target protein-binding efficiency. The Sips isotherm was used to assess the heterogeneity in Antibody affinity for the bispecific Antibody fragments. The results showed that the immobilized bispecific Antibody fragments exhibited an increased homogeneity of affinity (KD) to target molecules when compared with monospecific Antibody fragments immobilized by conventional methods. The…

  • Direct immobilization of gold-binding Antibody fragments for immunosensor applications
    Analytical Chemistry, 2010
    Co-Authors: Takahisa Ibii, Masaru Kaieda, Shuichiro Hatakeyama, Hidenori Shiotsuka, Hideki Watanabe, Mitsuo Umetsu, Izumi Kumagai, Takeshi Imamura

    Abstract:

    A novel method that enables Antibody fragments to be immobilized on a sensor substrate with a high binding capability using molecular recognition has been developed. Using genetic engineering, we fabricated bispecific recombinant Antibody fragments, which consist of two kinds of Antibody fragments: a gold Antibody fragment and a target molecule Antibody fragment. Surface plasmon resonance (SPR) analysis indicated that these gold-binding bispecific Antibody fragments bind directly to the gold substrate with high affinity (K(D) approximately 10(-9) M). About 70% of the bispecific Antibody fragments immobilized on the gold substrate retained their target protein-binding efficiency. The Sips isotherm was used to assess the heterogeneity in Antibody affinity for the bispecific Antibody fragments. The results showed that the immobilized bispecific Antibody fragments exhibited an increased homogeneity of affinity (K(D)) to target molecules when compared with monospecific Antibody fragments immobilized by conventional methods. The use of bispecific Antibody fragments to directly immobilize Antibody fragments on a solid-phase substrate offers a useful platform for immunosensor applications.

Beverly A Teicher – 3rd expert on this subject based on the ideXlab platform

  • What Can We Learn about Antibody-Drug Conjugates from the T-DM1 Experience?
    American Society of Clinical Oncology Educational Book, 2015
    Co-Authors: Francisco J. Esteva, Kathy D Miller, Beverly A Teicher

    Abstract:

    Antibody conjugates are a diverse class of therapeutics that consist of a cytotoxic agent linked covalently to an Antibody or Antibody fragment directed toward a specific cell surface target expressed by tumor cells. The notion that antibodies directed toward targets on the surface of malignant cells could be used for drug delivery is not new. The history of Antibody conjugates has been marked by hurdles identified and overcome. Early conjugates used mouse antibodies, drugs that either were not sufficiently potent, were immunogenic (proteins), or were too toxic, and linkers that were not sufficiently stable in circulation. Four main avenues have been explored using antibodies to target cytotoxic agents to malignant cells: Antibody-protein toxin (or Antibody fragment-protein toxin fusion) conjugates, Antibody-chelated radionuclide conjugates, Antibody-small molecule conjugates, and Antibody-enzyme conjugates administered along with small molecule prodrugs that require metabolism by the conjugated enzyme to release the activated species. Technology is continuing to evolve regarding the protein and small molecule components, and it is likely that single chemical entities soon will be the norm for Antibody-drug conjugates. Only Antibody-radionuclide conjugates and Antibody-drug conjugates have reached the regulatory approval stage, and there are more than 40 Antibody conjugates in clinical trials. The time may have come for this technology to become a major contributor to improving treatment for patients with cancer.

  • Antibody conjugate therapeutics challenges and potential
    Clinical Cancer Research, 2011
    Co-Authors: Beverly A Teicher, Ravi V J Chari

    Abstract:

    Antibody conjugates are a diverse class of therapeutics consisting of a cytotoxic agent linked covalently to an Antibody or Antibody fragment directed toward a specific cell surface target expressed by tumor cells. The notion that antibodies directed toward targets on the surface of malignant cells could be used for drug delivery is not new. The history of Antibody conjugates is marked by hurdles that have been identified and overcome. Early conjugates used mouse antibodies; cytotoxic agents that were immunogenic (proteins), too toxic, or not sufficiently potent; and linkers that were not sufficiently stable in circulation. Investigators have explored 4 main avenues using antibodies to target cytotoxic agents to malignant cells: Antibody-protein toxin (or Antibody fragment–protein toxin fusion) conjugates, Antibody-chelated radionuclide conjugates, Antibody–small-molecule drug conjugates, and Antibody-enzyme conjugates administered along with small-molecule prodrugs that require metabolism by the conjugated enzyme to release the activated species. Only Antibody-radionuclide conjugates and Antibody-drug conjugates have reached the regulatory approval stage, and nearly 20 Antibody conjugates are currently in clinical trials. The time may have come for this technology to become a major contributor to improving treatment for cancer patients. Clin Cancer Res; 17(20); 6389–97. ©2011 AACR .

  • Antibody conjugate therapeutics: Challenges and potential
    Clinical Cancer Research, 2011
    Co-Authors: Beverly A Teicher, Ravi V J Chari

    Abstract:

    Antibody conjugates are a diverse class of therapeutics consisting of a cytotoxic agent linked covalently to an Antibody or Antibody fragment directed toward a specific cell surface target expressed by tumor cells. The notion that antibodies directed toward targets on the surface of malignant cells could be used for drug delivery is not new. The history of Antibody conjugates is marked by hurdles that have been identified and overcome. Early conjugates used mouse antibodies; cytotoxic agents that were immunogenic (proteins), too toxic, or not sufficiently potent; and linkers that were not sufficiently stable in circulation. Investigators have explored 4 main avenues using antibodies to target cytotoxic agents to malignant cells: Antibody-protein toxin (or Antibody fragment-protein toxin fusion) conjugates, Antibody-chelated radionuclide conjugates, Antibody-small-molecule drug conjugates, and Antibody-enzyme conjugates administered along with small-molecule prodrugs that require metabolism by the conjugated enzyme to release the activated species. Only Antibody-radionuclide conjugates and Antibody-drug conjugates have reached the regulatory approval stage, and nearly 20 Antibody conjugates are currently in clinical trials. The time may have come for this technology to become a major contributor to improving treatment for cancer patients.