The Experts below are selected from a list of 15747 Experts worldwide ranked by ideXlab platform

Tanja Lövgren - One of the best experts on this subject based on the ideXlab platform.

  • synthetic single framework Antibody Library integrated with rapid affinity maturation by vl shuffling
    Protein Engineering Design & Selection, 2011
    Co-Authors: Eeva-christine Brockmann, T. Savukoski, A. Lehmusvuori, O. Saavalainen, Sultana Akter, Janne Leivo, Tuomas Huovinen, Alex Azhayev, Tanja Lövgren
    Abstract:

    Affinity maturation is often applied to improve the properties of antibodies isolated from universal Antibody libraries in vitro. A synthetic human scFv Antibody Library was constructed in single immunoglobulin framework to enable rapid affinity maturation by updated Kunkel's mutagenesis. The initial diversity was generated predominantly in the V(H) domain combined with only 36 V(L) domain variants yielding 3 × 10(10) unique members in the phage-displayed Library. After three rounds of panning the enriched V(H) genes from the primary Library selections against lysozyme were incorporated into a ready-made circular single-stranded affinity maturation Library containing 7 × 10(8) V(L) gene variants. Several unique antibodies with 0.8-10 nM (K(d), dissociation constant) affinities against lysozyme were found after panning from the affinity maturation Library, contrasted by only one anti-lysozyme scFv clone with K(d) <20 nM among the clones panned from the primary universal Library. The presented single-framework strategy provides a way to convey significant amount of functional V(H) domain diversity to affinity maturation without bimolecular ligation leading to a diverse set of antibodies with binding affinities in the low nanomolar range.

  • Synthetic single-framework Antibody Library integrated with rapid affinity maturation by VL shuffling
    Protein Engineering Design and Selection, 2011
    Co-Authors: Eeva-christine Brockmann, T. Savukoski, A. Lehmusvuori, O. Saavalainen, Sultana Akter, Janne Leivo, Tuomas Huovinen, Tanja Lövgren, Alex Azhayev, Shahriar Akter, Jukka Hellman
    Abstract:

    Affinity maturation is often applied to improve the properties of antibodies isolated from universal Antibody libraries in vitro. A synthetic human scFv Antibody Library was constructed in single immunoglobulin framework to enable rapid affinity maturation by updated Kunkel's mutagenesis. The initial diversity was generated predominantly in the V(H) domain combined with only 36 V(L) domain variants yielding 3 × 10(10) unique members in the phage-displayed Library. After three rounds of panning the enriched V(H) genes from the primary Library selections against lysozyme were incorporated into a ready-made circular single-stranded affinity maturation Library containing 7 × 10(8) V(L) gene variants. Several unique antibodies with 0.8-10 nM (K(d), dissociation constant) affinities against lysozyme were found after panning from the affinity maturation Library, contrasted by only one anti-lysozyme scFv clone with K(d)

O. Saavalainen - One of the best experts on this subject based on the ideXlab platform.

  • synthetic single framework Antibody Library integrated with rapid affinity maturation by vl shuffling
    Protein Engineering Design & Selection, 2011
    Co-Authors: Eeva-christine Brockmann, T. Savukoski, A. Lehmusvuori, O. Saavalainen, Sultana Akter, Janne Leivo, Tuomas Huovinen, Alex Azhayev, Tanja Lövgren
    Abstract:

    Affinity maturation is often applied to improve the properties of antibodies isolated from universal Antibody libraries in vitro. A synthetic human scFv Antibody Library was constructed in single immunoglobulin framework to enable rapid affinity maturation by updated Kunkel's mutagenesis. The initial diversity was generated predominantly in the V(H) domain combined with only 36 V(L) domain variants yielding 3 × 10(10) unique members in the phage-displayed Library. After three rounds of panning the enriched V(H) genes from the primary Library selections against lysozyme were incorporated into a ready-made circular single-stranded affinity maturation Library containing 7 × 10(8) V(L) gene variants. Several unique antibodies with 0.8-10 nM (K(d), dissociation constant) affinities against lysozyme were found after panning from the affinity maturation Library, contrasted by only one anti-lysozyme scFv clone with K(d) <20 nM among the clones panned from the primary universal Library. The presented single-framework strategy provides a way to convey significant amount of functional V(H) domain diversity to affinity maturation without bimolecular ligation leading to a diverse set of antibodies with binding affinities in the low nanomolar range.

  • Synthetic single-framework Antibody Library integrated with rapid affinity maturation by VL shuffling
    Protein Engineering Design and Selection, 2011
    Co-Authors: Eeva-christine Brockmann, T. Savukoski, A. Lehmusvuori, O. Saavalainen, Sultana Akter, Janne Leivo, Tuomas Huovinen, Tanja Lövgren, Alex Azhayev, Shahriar Akter, Jukka Hellman
    Abstract:

    Affinity maturation is often applied to improve the properties of antibodies isolated from universal Antibody libraries in vitro. A synthetic human scFv Antibody Library was constructed in single immunoglobulin framework to enable rapid affinity maturation by updated Kunkel's mutagenesis. The initial diversity was generated predominantly in the V(H) domain combined with only 36 V(L) domain variants yielding 3 × 10(10) unique members in the phage-displayed Library. After three rounds of panning the enriched V(H) genes from the primary Library selections against lysozyme were incorporated into a ready-made circular single-stranded affinity maturation Library containing 7 × 10(8) V(L) gene variants. Several unique antibodies with 0.8-10 nM (K(d), dissociation constant) affinities against lysozyme were found after panning from the affinity maturation Library, contrasted by only one anti-lysozyme scFv clone with K(d)

Eeva-christine Brockmann - One of the best experts on this subject based on the ideXlab platform.

  • synthetic single framework Antibody Library integrated with rapid affinity maturation by vl shuffling
    Protein Engineering Design & Selection, 2011
    Co-Authors: Eeva-christine Brockmann, T. Savukoski, A. Lehmusvuori, O. Saavalainen, Sultana Akter, Janne Leivo, Tuomas Huovinen, Alex Azhayev, Tanja Lövgren
    Abstract:

    Affinity maturation is often applied to improve the properties of antibodies isolated from universal Antibody libraries in vitro. A synthetic human scFv Antibody Library was constructed in single immunoglobulin framework to enable rapid affinity maturation by updated Kunkel's mutagenesis. The initial diversity was generated predominantly in the V(H) domain combined with only 36 V(L) domain variants yielding 3 × 10(10) unique members in the phage-displayed Library. After three rounds of panning the enriched V(H) genes from the primary Library selections against lysozyme were incorporated into a ready-made circular single-stranded affinity maturation Library containing 7 × 10(8) V(L) gene variants. Several unique antibodies with 0.8-10 nM (K(d), dissociation constant) affinities against lysozyme were found after panning from the affinity maturation Library, contrasted by only one anti-lysozyme scFv clone with K(d) <20 nM among the clones panned from the primary universal Library. The presented single-framework strategy provides a way to convey significant amount of functional V(H) domain diversity to affinity maturation without bimolecular ligation leading to a diverse set of antibodies with binding affinities in the low nanomolar range.

  • Synthetic single-framework Antibody Library integrated with rapid affinity maturation by VL shuffling
    Protein Engineering Design and Selection, 2011
    Co-Authors: Eeva-christine Brockmann, T. Savukoski, A. Lehmusvuori, O. Saavalainen, Sultana Akter, Janne Leivo, Tuomas Huovinen, Tanja Lövgren, Alex Azhayev, Shahriar Akter, Jukka Hellman
    Abstract:

    Affinity maturation is often applied to improve the properties of antibodies isolated from universal Antibody libraries in vitro. A synthetic human scFv Antibody Library was constructed in single immunoglobulin framework to enable rapid affinity maturation by updated Kunkel's mutagenesis. The initial diversity was generated predominantly in the V(H) domain combined with only 36 V(L) domain variants yielding 3 × 10(10) unique members in the phage-displayed Library. After three rounds of panning the enriched V(H) genes from the primary Library selections against lysozyme were incorporated into a ready-made circular single-stranded affinity maturation Library containing 7 × 10(8) V(L) gene variants. Several unique antibodies with 0.8-10 nM (K(d), dissociation constant) affinities against lysozyme were found after panning from the affinity maturation Library, contrasted by only one anti-lysozyme scFv clone with K(d)

Jukka Hellman - One of the best experts on this subject based on the ideXlab platform.

  • Synthetic single-framework Antibody Library integrated with rapid affinity maturation by VL shuffling
    Protein Engineering Design and Selection, 2011
    Co-Authors: Eeva-christine Brockmann, T. Savukoski, A. Lehmusvuori, O. Saavalainen, Sultana Akter, Janne Leivo, Tuomas Huovinen, Tanja Lövgren, Alex Azhayev, Shahriar Akter, Jukka Hellman
    Abstract:

    Affinity maturation is often applied to improve the properties of antibodies isolated from universal Antibody libraries in vitro. A synthetic human scFv Antibody Library was constructed in single immunoglobulin framework to enable rapid affinity maturation by updated Kunkel's mutagenesis. The initial diversity was generated predominantly in the V(H) domain combined with only 36 V(L) domain variants yielding 3 × 10(10) unique members in the phage-displayed Library. After three rounds of panning the enriched V(H) genes from the primary Library selections against lysozyme were incorporated into a ready-made circular single-stranded affinity maturation Library containing 7 × 10(8) V(L) gene variants. Several unique antibodies with 0.8-10 nM (K(d), dissociation constant) affinities against lysozyme were found after panning from the affinity maturation Library, contrasted by only one anti-lysozyme scFv clone with K(d)

Sultana Akter - One of the best experts on this subject based on the ideXlab platform.

  • synthetic single framework Antibody Library integrated with rapid affinity maturation by vl shuffling
    Protein Engineering Design & Selection, 2011
    Co-Authors: Eeva-christine Brockmann, T. Savukoski, A. Lehmusvuori, O. Saavalainen, Sultana Akter, Janne Leivo, Tuomas Huovinen, Alex Azhayev, Tanja Lövgren
    Abstract:

    Affinity maturation is often applied to improve the properties of antibodies isolated from universal Antibody libraries in vitro. A synthetic human scFv Antibody Library was constructed in single immunoglobulin framework to enable rapid affinity maturation by updated Kunkel's mutagenesis. The initial diversity was generated predominantly in the V(H) domain combined with only 36 V(L) domain variants yielding 3 × 10(10) unique members in the phage-displayed Library. After three rounds of panning the enriched V(H) genes from the primary Library selections against lysozyme were incorporated into a ready-made circular single-stranded affinity maturation Library containing 7 × 10(8) V(L) gene variants. Several unique antibodies with 0.8-10 nM (K(d), dissociation constant) affinities against lysozyme were found after panning from the affinity maturation Library, contrasted by only one anti-lysozyme scFv clone with K(d) <20 nM among the clones panned from the primary universal Library. The presented single-framework strategy provides a way to convey significant amount of functional V(H) domain diversity to affinity maturation without bimolecular ligation leading to a diverse set of antibodies with binding affinities in the low nanomolar range.

  • Synthetic single-framework Antibody Library integrated with rapid affinity maturation by VL shuffling
    Protein Engineering Design and Selection, 2011
    Co-Authors: Eeva-christine Brockmann, T. Savukoski, A. Lehmusvuori, O. Saavalainen, Sultana Akter, Janne Leivo, Tuomas Huovinen, Tanja Lövgren, Alex Azhayev, Shahriar Akter, Jukka Hellman
    Abstract:

    Affinity maturation is often applied to improve the properties of antibodies isolated from universal Antibody libraries in vitro. A synthetic human scFv Antibody Library was constructed in single immunoglobulin framework to enable rapid affinity maturation by updated Kunkel's mutagenesis. The initial diversity was generated predominantly in the V(H) domain combined with only 36 V(L) domain variants yielding 3 × 10(10) unique members in the phage-displayed Library. After three rounds of panning the enriched V(H) genes from the primary Library selections against lysozyme were incorporated into a ready-made circular single-stranded affinity maturation Library containing 7 × 10(8) V(L) gene variants. Several unique antibodies with 0.8-10 nM (K(d), dissociation constant) affinities against lysozyme were found after panning from the affinity maturation Library, contrasted by only one anti-lysozyme scFv clone with K(d)