The Experts below are selected from a list of 186 Experts worldwide ranked by ideXlab platform
Manfred Auer - One of the best experts on this subject based on the ideXlab platform.
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on bead screens sample narrower affinity ranges of protein ligand interactions compared to Equivalent Solution assays
ChemPhysChem, 2012Co-Authors: Martin Hintersteiner, Christof Buehler, Manfred AuerAbstract:Conceptually, on-bead screening is one of the most efficient high-throughput screening (HTS) methods. One of its inherent advantages is that the solid support has a dual function: it serves as a synthesis platform and as a screening compartment. Compound purification, cleavage and storage and extensive liquid handling are not necessary in bead-based HTS. Since the establishment of one-bead one-compound library synthesis, the properties of polymer beads in chemical reactions have been thoroughly investigated. However, the characterization of the kinetics and thermodynamics of protein-ligand interactions on the beads used for screening has received much less attention. Consequently, the majority of reported on-bead screens are based on empirically derived procedures, independent of measured equilibrium constants and rate constants of protein binding to ligands on beads. More often than not, on-bead screens reveal apparent high affinity binders through strong protein complexation on the matrix of the solid support. After decoding, resynthesis, and Solution testing the primary hits turn out to be unexpectedly weak binders, or may even fall out of the detection limit of the Solution assay. Only a quantitative comparison of on-bead binding and Solution binding events will allow systematically investigating affinity differences as function of protein and small molecule properties. This will open up routes for optimized bead materials, blocking conditions and other improved assay procedures. By making use of the unique features of our previously introduced confocal nanoscanning (CONA) method, we investigated the kinetic and thermodynamic properties of protein-ligand interactions on TentaGel beads, a popular solid support for on-bead screening. The data obtained from these experiments allowed us to determine dissociation constants for the interaction of bead-immobilized ligands with soluble proteins. Our results therefore provide, for the first time, a comparison of on-bead versus Solution binding thermodynamics. Our data indicate that affinity ranges found in on-bead screening are indeed narrower compared to Equivalent interactions in homogeneous Solution. A thorough physico-chemical understanding of the molecular recognition between proteins and surface bound ligands will further strengthen the role of on-bead screening as an ultimately cost-effective method in hit and lead finding.
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On‐Bead Screens Sample Narrower Affinity Ranges of Protein–Ligand Interactions Compared to Equivalent Solution Assays
Chemphyschem : a European journal of chemical physics and physical chemistry, 2012Co-Authors: Martin Hintersteiner, Christof Buehler, Manfred AuerAbstract:Conceptually, on-bead screening is one of the most efficient high-throughput screening (HTS) methods. One of its inherent advantages is that the solid support has a dual function: it serves as a synthesis platform and as a screening compartment. Compound purification, cleavage and storage and extensive liquid handling are not necessary in bead-based HTS. Since the establishment of one-bead one-compound library synthesis, the properties of polymer beads in chemical reactions have been thoroughly investigated. However, the characterization of the kinetics and thermodynamics of protein-ligand interactions on the beads used for screening has received much less attention. Consequently, the majority of reported on-bead screens are based on empirically derived procedures, independent of measured equilibrium constants and rate constants of protein binding to ligands on beads. More often than not, on-bead screens reveal apparent high affinity binders through strong protein complexation on the matrix of the solid support. After decoding, resynthesis, and Solution testing the primary hits turn out to be unexpectedly weak binders, or may even fall out of the detection limit of the Solution assay. Only a quantitative comparison of on-bead binding and Solution binding events will allow systematically investigating affinity differences as function of protein and small molecule properties. This will open up routes for optimized bead materials, blocking conditions and other improved assay procedures. By making use of the unique features of our previously introduced confocal nanoscanning (CONA) method, we investigated the kinetic and thermodynamic properties of protein-ligand interactions on TentaGel beads, a popular solid support for on-bead screening. The data obtained from these experiments allowed us to determine dissociation constants for the interaction of bead-immobilized ligands with soluble proteins. Our results therefore provide, for the first time, a comparison of on-bead versus Solution binding thermodynamics. Our data indicate that affinity ranges found in on-bead screening are indeed narrower compared to Equivalent interactions in homogeneous Solution. A thorough physico-chemical understanding of the molecular recognition between proteins and surface bound ligands will further strengthen the role of on-bead screening as an ultimately cost-effective method in hit and lead finding.
Martin Hintersteiner - One of the best experts on this subject based on the ideXlab platform.
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on bead screens sample narrower affinity ranges of protein ligand interactions compared to Equivalent Solution assays
ChemPhysChem, 2012Co-Authors: Martin Hintersteiner, Christof Buehler, Manfred AuerAbstract:Conceptually, on-bead screening is one of the most efficient high-throughput screening (HTS) methods. One of its inherent advantages is that the solid support has a dual function: it serves as a synthesis platform and as a screening compartment. Compound purification, cleavage and storage and extensive liquid handling are not necessary in bead-based HTS. Since the establishment of one-bead one-compound library synthesis, the properties of polymer beads in chemical reactions have been thoroughly investigated. However, the characterization of the kinetics and thermodynamics of protein-ligand interactions on the beads used for screening has received much less attention. Consequently, the majority of reported on-bead screens are based on empirically derived procedures, independent of measured equilibrium constants and rate constants of protein binding to ligands on beads. More often than not, on-bead screens reveal apparent high affinity binders through strong protein complexation on the matrix of the solid support. After decoding, resynthesis, and Solution testing the primary hits turn out to be unexpectedly weak binders, or may even fall out of the detection limit of the Solution assay. Only a quantitative comparison of on-bead binding and Solution binding events will allow systematically investigating affinity differences as function of protein and small molecule properties. This will open up routes for optimized bead materials, blocking conditions and other improved assay procedures. By making use of the unique features of our previously introduced confocal nanoscanning (CONA) method, we investigated the kinetic and thermodynamic properties of protein-ligand interactions on TentaGel beads, a popular solid support for on-bead screening. The data obtained from these experiments allowed us to determine dissociation constants for the interaction of bead-immobilized ligands with soluble proteins. Our results therefore provide, for the first time, a comparison of on-bead versus Solution binding thermodynamics. Our data indicate that affinity ranges found in on-bead screening are indeed narrower compared to Equivalent interactions in homogeneous Solution. A thorough physico-chemical understanding of the molecular recognition between proteins and surface bound ligands will further strengthen the role of on-bead screening as an ultimately cost-effective method in hit and lead finding.
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On‐Bead Screens Sample Narrower Affinity Ranges of Protein–Ligand Interactions Compared to Equivalent Solution Assays
Chemphyschem : a European journal of chemical physics and physical chemistry, 2012Co-Authors: Martin Hintersteiner, Christof Buehler, Manfred AuerAbstract:Conceptually, on-bead screening is one of the most efficient high-throughput screening (HTS) methods. One of its inherent advantages is that the solid support has a dual function: it serves as a synthesis platform and as a screening compartment. Compound purification, cleavage and storage and extensive liquid handling are not necessary in bead-based HTS. Since the establishment of one-bead one-compound library synthesis, the properties of polymer beads in chemical reactions have been thoroughly investigated. However, the characterization of the kinetics and thermodynamics of protein-ligand interactions on the beads used for screening has received much less attention. Consequently, the majority of reported on-bead screens are based on empirically derived procedures, independent of measured equilibrium constants and rate constants of protein binding to ligands on beads. More often than not, on-bead screens reveal apparent high affinity binders through strong protein complexation on the matrix of the solid support. After decoding, resynthesis, and Solution testing the primary hits turn out to be unexpectedly weak binders, or may even fall out of the detection limit of the Solution assay. Only a quantitative comparison of on-bead binding and Solution binding events will allow systematically investigating affinity differences as function of protein and small molecule properties. This will open up routes for optimized bead materials, blocking conditions and other improved assay procedures. By making use of the unique features of our previously introduced confocal nanoscanning (CONA) method, we investigated the kinetic and thermodynamic properties of protein-ligand interactions on TentaGel beads, a popular solid support for on-bead screening. The data obtained from these experiments allowed us to determine dissociation constants for the interaction of bead-immobilized ligands with soluble proteins. Our results therefore provide, for the first time, a comparison of on-bead versus Solution binding thermodynamics. Our data indicate that affinity ranges found in on-bead screening are indeed narrower compared to Equivalent interactions in homogeneous Solution. A thorough physico-chemical understanding of the molecular recognition between proteins and surface bound ligands will further strengthen the role of on-bead screening as an ultimately cost-effective method in hit and lead finding.
Zhang Beidou - One of the best experts on this subject based on the ideXlab platform.
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An Equivalent Solution for the electromagnetic scattering of multilayer particle
Journal of Quantitative Spectroscopy and Radiative Transfer, 2013Co-Authors: Li Xingcai, Zhang BeidouAbstract:Abstract This paper reports on a new Solution to the scattering properties of a small multilayer particle. The procedure is based on a prescription which uses the Equivalent dielectric constant to represent the integrated permittivity of the multilayer particle, and then directly get the particle's scattering properties with the classical Mie code. By means of comparisons of the proposed method and the multilayer Mie Solutions, it is evident that the model presented in this paper is accurate and more simple.
Christof Buehler - One of the best experts on this subject based on the ideXlab platform.
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on bead screens sample narrower affinity ranges of protein ligand interactions compared to Equivalent Solution assays
ChemPhysChem, 2012Co-Authors: Martin Hintersteiner, Christof Buehler, Manfred AuerAbstract:Conceptually, on-bead screening is one of the most efficient high-throughput screening (HTS) methods. One of its inherent advantages is that the solid support has a dual function: it serves as a synthesis platform and as a screening compartment. Compound purification, cleavage and storage and extensive liquid handling are not necessary in bead-based HTS. Since the establishment of one-bead one-compound library synthesis, the properties of polymer beads in chemical reactions have been thoroughly investigated. However, the characterization of the kinetics and thermodynamics of protein-ligand interactions on the beads used for screening has received much less attention. Consequently, the majority of reported on-bead screens are based on empirically derived procedures, independent of measured equilibrium constants and rate constants of protein binding to ligands on beads. More often than not, on-bead screens reveal apparent high affinity binders through strong protein complexation on the matrix of the solid support. After decoding, resynthesis, and Solution testing the primary hits turn out to be unexpectedly weak binders, or may even fall out of the detection limit of the Solution assay. Only a quantitative comparison of on-bead binding and Solution binding events will allow systematically investigating affinity differences as function of protein and small molecule properties. This will open up routes for optimized bead materials, blocking conditions and other improved assay procedures. By making use of the unique features of our previously introduced confocal nanoscanning (CONA) method, we investigated the kinetic and thermodynamic properties of protein-ligand interactions on TentaGel beads, a popular solid support for on-bead screening. The data obtained from these experiments allowed us to determine dissociation constants for the interaction of bead-immobilized ligands with soluble proteins. Our results therefore provide, for the first time, a comparison of on-bead versus Solution binding thermodynamics. Our data indicate that affinity ranges found in on-bead screening are indeed narrower compared to Equivalent interactions in homogeneous Solution. A thorough physico-chemical understanding of the molecular recognition between proteins and surface bound ligands will further strengthen the role of on-bead screening as an ultimately cost-effective method in hit and lead finding.
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On‐Bead Screens Sample Narrower Affinity Ranges of Protein–Ligand Interactions Compared to Equivalent Solution Assays
Chemphyschem : a European journal of chemical physics and physical chemistry, 2012Co-Authors: Martin Hintersteiner, Christof Buehler, Manfred AuerAbstract:Conceptually, on-bead screening is one of the most efficient high-throughput screening (HTS) methods. One of its inherent advantages is that the solid support has a dual function: it serves as a synthesis platform and as a screening compartment. Compound purification, cleavage and storage and extensive liquid handling are not necessary in bead-based HTS. Since the establishment of one-bead one-compound library synthesis, the properties of polymer beads in chemical reactions have been thoroughly investigated. However, the characterization of the kinetics and thermodynamics of protein-ligand interactions on the beads used for screening has received much less attention. Consequently, the majority of reported on-bead screens are based on empirically derived procedures, independent of measured equilibrium constants and rate constants of protein binding to ligands on beads. More often than not, on-bead screens reveal apparent high affinity binders through strong protein complexation on the matrix of the solid support. After decoding, resynthesis, and Solution testing the primary hits turn out to be unexpectedly weak binders, or may even fall out of the detection limit of the Solution assay. Only a quantitative comparison of on-bead binding and Solution binding events will allow systematically investigating affinity differences as function of protein and small molecule properties. This will open up routes for optimized bead materials, blocking conditions and other improved assay procedures. By making use of the unique features of our previously introduced confocal nanoscanning (CONA) method, we investigated the kinetic and thermodynamic properties of protein-ligand interactions on TentaGel beads, a popular solid support for on-bead screening. The data obtained from these experiments allowed us to determine dissociation constants for the interaction of bead-immobilized ligands with soluble proteins. Our results therefore provide, for the first time, a comparison of on-bead versus Solution binding thermodynamics. Our data indicate that affinity ranges found in on-bead screening are indeed narrower compared to Equivalent interactions in homogeneous Solution. A thorough physico-chemical understanding of the molecular recognition between proteins and surface bound ligands will further strengthen the role of on-bead screening as an ultimately cost-effective method in hit and lead finding.
Li Xingcai - One of the best experts on this subject based on the ideXlab platform.
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An Equivalent Solution for the electromagnetic scattering of multilayer particle
Journal of Quantitative Spectroscopy and Radiative Transfer, 2013Co-Authors: Li Xingcai, Zhang BeidouAbstract:Abstract This paper reports on a new Solution to the scattering properties of a small multilayer particle. The procedure is based on a prescription which uses the Equivalent dielectric constant to represent the integrated permittivity of the multilayer particle, and then directly get the particle's scattering properties with the classical Mie code. By means of comparisons of the proposed method and the multilayer Mie Solutions, it is evident that the model presented in this paper is accurate and more simple.