The Experts below are selected from a list of 264 Experts worldwide ranked by ideXlab platform
Gerhard Kopperschläger - One of the best experts on this subject based on the ideXlab platform.
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Epitope mapping of a monoclonal antibody directed against the α-subunit of phosphofructokinase-1 from Saccharomyces cerevisiae by screening phage display libraries
Journal of Molecular Recognition, 1999Co-Authors: Margrit Hollborn, Gerd Birkenmeier, Jürgen Kirchberger, Gerhard KopperschlägerAbstract:Phosphofructokinase-1 from Saccharomyces cerevisiae is composed of two types of subunits, alpha and beta. Subunit-specific monoclonal antibodies were raised to elucidate structural and functional properties of both subunits. One monoclonal antibody, alpha-F3, binds to an epitope either at the C-terminal or at the N-terminal part of the alpha-polypeptide chain. By screening a Heptapeptide library with this monoclonal antibody, a set of Heptapeptides was selected, which contained the consensus sequences D-A-F and D-S-F. Two Heptapeptides with these motifs were synthesized in order assess their capacity to inhibit the binding of antibody alpha-F3 to native phosphofructokinase-1. The peptide G-I-K-D-A-F-L inhibited the binding more strongly (IC50 = 1.5 microM) than the peptide A-P-W-H-D-S-F (IC50 = 33.3 microM). Sequence matching revealed the presence of the D-A-F motif in the polypeptide chain of phosphofructokinase-1 at amino acid position 172-174. As a control, the nonapeptide A-P-T-S-K-D-A-F-L which corresponds to the sequence of the putative epitope was tested in the inhibition assay. In view of the high inhibitory capacity (IC50 = 0.3 microM) it was concluded that this nonapeptide represents the continuous epitope of phosphofructokinase-1 that is recognized by antibody alpha-F3.
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EPITOPE MAPPING OF A MONOCLONAL ANTIBODY DIRECTED AGAINST THE ALPHA -SUBUNIT OF PHOSPHOFRUCTOKINASE-1 FROM SACCHAROMYCES CEREVISIAE BY SCREENING PHAGE DISPLAY LIBRARIES
Journal of Molecular Recognition, 1999Co-Authors: Margrit Hollborn, Gerd Birkenmeier, Jürgen Kirchberger, Gerhard KopperschlägerAbstract:Phosphofructokinase-1 from Saccharomyces cerevisiae is composed of two types of subunits, α and β. Subunit-specific monoclonal antibodies were raised to elucidate structural and functional properties of both subunits. One monoclonal antibody, α-F3, binds to an epitope either at the C-terminal or at the N-terminal part of the α-polypeptide chain. By screening a Heptapeptide library with this monoclonal antibody, a set of Heptapeptides was selected, which contained the consensus sequences D–A–F and D–S–F. Two Heptapeptides with these motifs were synthesized in order assess their capacity to inhibit the binding of antibody α-F3 to native phosphofructokinase-1. The peptide G–I–K–D–A–F–L inhibited the binding more strongly (IC50 = 1.5 µM) than the peptide A–P–W–H–D–S–F (IC50 = 33.3 µM). Sequence matching revealed the presence of the D–A–F motif in the polypeptide chain of phosphofructokinase-1 at amino acid position 172–174. As a control, the nonapeptide A–P–T–S–K–D–A–F–L which corresponds to the sequence of the putative epitope was tested in the inhibition assay. In view of the high inhibitory capacity (IC50 = 0.3 µM) it was concluded that this nonapeptide represents the continuous epitope of phosphofructokinase-1 that is recognized by antibody α-F3. Copyright © 1999 John Wiley & Sons, Ltd.
Alan R Katritzky - One of the best experts on this subject based on the ideXlab platform.
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total synthesis of cyclic Heptapeptide rolloamide b
Chemical Communications, 2013Co-Authors: Mirna El Khatib, Mohamed Elagawany, Eray Caliskan, Emily Faith Davis, Hassan M Faidallah, Said A Elfeky, Alan R KatritzkyAbstract:The first total synthesis of Rolloamide B, a cyclic proline-enriched Heptapeptide, is reported. This work features solution phase benzotriazole-mediated peptide synthesis ligating native amino acids.
Karen Shires - One of the best experts on this subject based on the ideXlab platform.
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serine and proline rich ligands enriched via phage display technology show preferential binding to bcr abl expressing cells
Hematology Oncology and Stem Cell Therapy, 2014Co-Authors: Karen Shires, Iva Shankland, Shaheen Mowla, Samuel Njikan, Jai Jaymacker, Nicolas NovitzkyAbstract:Background and objectives Despite the use of targeted therapy, chronic myelogenous leukemia (CML) currently remains incurable with drug therapy, with patients requiring life-long treatment. Developing either a vaccine to prevent the disease or another novel drug to specifically target and eradicate the CML cell will require the identification of CML-associated cell-surface markers and molecules that can bind specifically to the cell surface. In an attempt to discover peptides that bind specifically to cells in the early chronic phase of the disease, we used phage-display technology to identify Heptapeptides that bind specifically to the surface of BCR/ABL-expressing fibroblasts. Methods An in vitro system using NIH3T3 stably transfected with pGD210 (BCR/ABL) was used as a model for the chronic phase of the disease. The cells were panned using a linear Heptapeptide phage library (Ph.D 7.0) in a negative/positive panning strategy with NIH3T3 containing only the plasmid vector as the wild type control. Results We identified four novel peptides that were enriched through this technique. These peptides contained either multiple proline residues or serine/threonine–proline pairs and showed a confirmed binding preference for BCR/ABL+ fibroblasts. The peptide Y-R-A-P-W-P-P also showed a binding affinity for granulocytes from untreated CML patients. Conclusion We have identified several novel peptides that can be used in future studies to identify specific CML cell-surface antigens or provide a novel drug-delivery mechanism.
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Serine and proline-rich ligands enriched via phage-display technology show preferential binding to BCR/ABL expressing cells
Hematology Oncology and Stem Cell Therapy, 2014Co-Authors: Karen Shires, Iva Shankland, Shaheen Mowla, Samuel Njikan, Jai Jaymacker, Nicolas NovitzkyAbstract:Background and objectives Despite the use of targeted therapy, chronic myelogenous leukemia (CML) currently remains incurable with drug therapy, with patients requiring life-long treatment. Developing either a vaccine to prevent the disease or another novel drug to specifically target and eradicate the CML cell will require the identification of CML-associated cell-surface markers and molecules that can bind specifically to the cell surface. In an attempt to discover peptides that bind specifically to cells in the early chronic phase of the disease, we used phage-display technology to identify Heptapeptides that bind specifically to the surface of BCR/ABL-expressing fibroblasts. Methods An in vitro system using NIH3T3 stably transfected with pGD210 (BCR/ABL) was used as a model for the chronic phase of the disease. The cells were panned using a linear Heptapeptide phage library (Ph.D 7.0) in a negative/positive panning strategy with NIH3T3 containing only the plasmid vector as the wild type control. Results We identified four novel peptides that were enriched through this technique. These peptides contained either multiple proline residues or serine/threonine–proline pairs and showed a confirmed binding preference for BCR/ABL+ fibroblasts. The peptide Y-R-A-P-W-P-P also showed a binding affinity for granulocytes from untreated CML patients. Conclusion We have identified several novel peptides that can be used in future studies to identify specific CML cell-surface antigens or provide a novel drug-delivery mechanism.
Nicolas Novitzky - One of the best experts on this subject based on the ideXlab platform.
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serine and proline rich ligands enriched via phage display technology show preferential binding to bcr abl expressing cells
Hematology Oncology and Stem Cell Therapy, 2014Co-Authors: Karen Shires, Iva Shankland, Shaheen Mowla, Samuel Njikan, Jai Jaymacker, Nicolas NovitzkyAbstract:Background and objectives Despite the use of targeted therapy, chronic myelogenous leukemia (CML) currently remains incurable with drug therapy, with patients requiring life-long treatment. Developing either a vaccine to prevent the disease or another novel drug to specifically target and eradicate the CML cell will require the identification of CML-associated cell-surface markers and molecules that can bind specifically to the cell surface. In an attempt to discover peptides that bind specifically to cells in the early chronic phase of the disease, we used phage-display technology to identify Heptapeptides that bind specifically to the surface of BCR/ABL-expressing fibroblasts. Methods An in vitro system using NIH3T3 stably transfected with pGD210 (BCR/ABL) was used as a model for the chronic phase of the disease. The cells were panned using a linear Heptapeptide phage library (Ph.D 7.0) in a negative/positive panning strategy with NIH3T3 containing only the plasmid vector as the wild type control. Results We identified four novel peptides that were enriched through this technique. These peptides contained either multiple proline residues or serine/threonine–proline pairs and showed a confirmed binding preference for BCR/ABL+ fibroblasts. The peptide Y-R-A-P-W-P-P also showed a binding affinity for granulocytes from untreated CML patients. Conclusion We have identified several novel peptides that can be used in future studies to identify specific CML cell-surface antigens or provide a novel drug-delivery mechanism.
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Serine and proline-rich ligands enriched via phage-display technology show preferential binding to BCR/ABL expressing cells
Hematology Oncology and Stem Cell Therapy, 2014Co-Authors: Karen Shires, Iva Shankland, Shaheen Mowla, Samuel Njikan, Jai Jaymacker, Nicolas NovitzkyAbstract:Background and objectives Despite the use of targeted therapy, chronic myelogenous leukemia (CML) currently remains incurable with drug therapy, with patients requiring life-long treatment. Developing either a vaccine to prevent the disease or another novel drug to specifically target and eradicate the CML cell will require the identification of CML-associated cell-surface markers and molecules that can bind specifically to the cell surface. In an attempt to discover peptides that bind specifically to cells in the early chronic phase of the disease, we used phage-display technology to identify Heptapeptides that bind specifically to the surface of BCR/ABL-expressing fibroblasts. Methods An in vitro system using NIH3T3 stably transfected with pGD210 (BCR/ABL) was used as a model for the chronic phase of the disease. The cells were panned using a linear Heptapeptide phage library (Ph.D 7.0) in a negative/positive panning strategy with NIH3T3 containing only the plasmid vector as the wild type control. Results We identified four novel peptides that were enriched through this technique. These peptides contained either multiple proline residues or serine/threonine–proline pairs and showed a confirmed binding preference for BCR/ABL+ fibroblasts. The peptide Y-R-A-P-W-P-P also showed a binding affinity for granulocytes from untreated CML patients. Conclusion We have identified several novel peptides that can be used in future studies to identify specific CML cell-surface antigens or provide a novel drug-delivery mechanism.
Margrit Hollborn - One of the best experts on this subject based on the ideXlab platform.
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Epitope mapping of a monoclonal antibody directed against the α-subunit of phosphofructokinase-1 from Saccharomyces cerevisiae by screening phage display libraries
Journal of Molecular Recognition, 1999Co-Authors: Margrit Hollborn, Gerd Birkenmeier, Jürgen Kirchberger, Gerhard KopperschlägerAbstract:Phosphofructokinase-1 from Saccharomyces cerevisiae is composed of two types of subunits, alpha and beta. Subunit-specific monoclonal antibodies were raised to elucidate structural and functional properties of both subunits. One monoclonal antibody, alpha-F3, binds to an epitope either at the C-terminal or at the N-terminal part of the alpha-polypeptide chain. By screening a Heptapeptide library with this monoclonal antibody, a set of Heptapeptides was selected, which contained the consensus sequences D-A-F and D-S-F. Two Heptapeptides with these motifs were synthesized in order assess their capacity to inhibit the binding of antibody alpha-F3 to native phosphofructokinase-1. The peptide G-I-K-D-A-F-L inhibited the binding more strongly (IC50 = 1.5 microM) than the peptide A-P-W-H-D-S-F (IC50 = 33.3 microM). Sequence matching revealed the presence of the D-A-F motif in the polypeptide chain of phosphofructokinase-1 at amino acid position 172-174. As a control, the nonapeptide A-P-T-S-K-D-A-F-L which corresponds to the sequence of the putative epitope was tested in the inhibition assay. In view of the high inhibitory capacity (IC50 = 0.3 microM) it was concluded that this nonapeptide represents the continuous epitope of phosphofructokinase-1 that is recognized by antibody alpha-F3.
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EPITOPE MAPPING OF A MONOCLONAL ANTIBODY DIRECTED AGAINST THE ALPHA -SUBUNIT OF PHOSPHOFRUCTOKINASE-1 FROM SACCHAROMYCES CEREVISIAE BY SCREENING PHAGE DISPLAY LIBRARIES
Journal of Molecular Recognition, 1999Co-Authors: Margrit Hollborn, Gerd Birkenmeier, Jürgen Kirchberger, Gerhard KopperschlägerAbstract:Phosphofructokinase-1 from Saccharomyces cerevisiae is composed of two types of subunits, α and β. Subunit-specific monoclonal antibodies were raised to elucidate structural and functional properties of both subunits. One monoclonal antibody, α-F3, binds to an epitope either at the C-terminal or at the N-terminal part of the α-polypeptide chain. By screening a Heptapeptide library with this monoclonal antibody, a set of Heptapeptides was selected, which contained the consensus sequences D–A–F and D–S–F. Two Heptapeptides with these motifs were synthesized in order assess their capacity to inhibit the binding of antibody α-F3 to native phosphofructokinase-1. The peptide G–I–K–D–A–F–L inhibited the binding more strongly (IC50 = 1.5 µM) than the peptide A–P–W–H–D–S–F (IC50 = 33.3 µM). Sequence matching revealed the presence of the D–A–F motif in the polypeptide chain of phosphofructokinase-1 at amino acid position 172–174. As a control, the nonapeptide A–P–T–S–K–D–A–F–L which corresponds to the sequence of the putative epitope was tested in the inhibition assay. In view of the high inhibitory capacity (IC50 = 0.3 µM) it was concluded that this nonapeptide represents the continuous epitope of phosphofructokinase-1 that is recognized by antibody α-F3. Copyright © 1999 John Wiley & Sons, Ltd.