Nature of Specific Ligand-Receptor Bonds, in Particular the Antigen-Antibody Bond

Cj, Van Oss

doi:10.1080/01971520009349531

Cited by 20 publications

(19 citation statements)

References 52 publications

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“…Both antibodies and antigens usually have complicated tertiary structures and need firm immobilization to the substrates. Their interactions depend on geometric factors, conformational state, and environment, and steric hindrance must be avoided (Davis and Padlan, 1990;Webster et al, 1994;Van Oss, 1994). The expected forces are in the piconewton range, and the antigenbinding sites of the antibodies are small compared with the antibody itself, so that nonspecific interactions must be considerated.…”

Section: Fluorescein / Anti-fluorescein Igg Interactionsmentioning

confidence: 99%

Measurements of the Forces in Protein Interactions with Atomic Force Microscopy

Lin

Chen²,

Huang³

et al. 2005

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Protein interactions with ligands or other proteins are controlled by a complex array of intermolecular forces. Although the interaction energies and intermolecular forces which contribute to the stabilization of the protein complex can be inferred indirectly from thermodynamic and kinetic approaches or be calculated with molecular simulation, recent progress in atomic force microscopy (AFM) has made it possible to quantify directly the ranges and magnitudes of the interaction forces between protein and other molecules. AFM has proved its value not only for resolving the topographical structure of protein samples, but also for probing the forces that control protein interactions or mechanical properties of proteins under physiological conditions. The objective of this review is to describe the uses of AFM in the determination of the forces that control biological interactions, focusing especially on protein-ligand and protein-protein interaction modes. We first consider measurements of the specific and the nonspecific forces that jointly control protein interactions. The review then indicates the theoretical background of AFM force curves and presents the great variety of force measurement modes that can be performed with this technique. In addition, some of the most recent studies in determining the unbinding forces and mechanical properties of proteins with AFM are reviewed and the available theoretical aspects necessary for the comprehension of the experiments have been provided.

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Section: Fluorescein / Anti-fluorescein Igg Interactionsmentioning

confidence: 99%

Measurements of the Forces in Protein Interactions with Atomic Force Microscopy

Lin

Chen²,

Huang³

et al. 2005

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“…Besides pool size, additional important parameters influencing dimer formation in an aqueous solution comprise pH value, ionic strength, chemical nature of additives, total IgG concentration, temperature and duration in the liquid state (reaction time) [8]. The underlying reversible IgG-IgG interactions contributing to the most part of dimerization can be assumed to be mainly based on electrostatic (Coulombic) and polar (electron-acceptorelectron-donor) forces of every conceivable proportion as known for the majority of ab-ag reactions [12].…”

Section: Indications Of Fab-fab Interactions During Dimer Formation: mentioning

confidence: 99%

IgG Dimers in Multidonor-Derived Immunoglobulins: Aspects of Generation and Function

Gronski¹

2006

CPD

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Immunoglobulin G (IgG) concentrates for therapeutic purposes, like passive immunotherapy, supplementation in inherited or acquired deficiencies or immunomodulation, are prepared from multidonor-derived plasma pools. They usually contain varying amounts of dimeric IgG. The essential factor influencing dimer formation is the pool size; in addition, molecular properties of IgG and a variety of production process- and formulation-specific parameters are important. Numerous experimental findings suggest that dimers are predominantly generated by interactions of idiotypic and anti-idiotypic antibodies (Ids, anti-Ids). Ab-inherent crossreactivity, frequency distribution of both the affinities for particular Id-anti-Id interactions and the corresponding dimer concentrations still have to be elucidated. All these parameters influencing molecular features and functional activity of IgG dimers hamper the assay-dependent measurement of biological efficacy and correlation of total IgG content. A more detailed understanding may help to better control the dual nature of dimer-dependent biological activity comprising both undesirable (e.g., hypotension) and desirable effects of dimeric IgG (blockade of the reticuloendothelial system, RES, in immune thrombocytopenic purpura, ITP). These effects are detectable in in vitro and in vivo models and are thought to be of relevance for humans.

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“…Such mobile phases are preferably based on volatile, low ionic strength buffers, which is in contrast to the physiological conditions encountered in the natural environment, e.g., in blood. Since antibody-ligand interactions are based on noncovalent forces that are sensitive to the environment in which binding takes place, 56,57 identification of a suitable buffer can potentially be a critical task. However, we found that the antibody-based CSPs are stable in a 0.1 mM ammonium bicarbonate buffer, which allowed interfacing of miniaturized columns with an MS detector.…”

Section: S16mentioning

confidence: 99%

New developments in the production and use of stereoselective antibodies

et al. 2005

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This article describes the production of stereoselective antibodies using both classical immunological and modern molecular biological techniques. Stereoselective antibodies against alpha-hydroxy acids were raised in rabbits and mice and compared with previously produced anti-alpha-amino acid antibodies. It was found that both types of antibodies combine stereoselectivity with class-specificity. Sequence analyses revealed that antibodies with opposing stereoselectivities can be formed during the affinity maturation process from a common progenitor or independently using nonhomologous binding sites. For the first time, phage display was employed to obtain stereoselective antibody fragments. The versatility of stereoselective antibodies as chiral selectors was demonstrated by applying them in several immunosensors and in chiral chromatography. A simple, membrane-based optical sensor allowed detection of enantiomeric impurities at the 1/2,000 level (99.9% ee). Silica-based antibody chiral stationary phases could be used for enantiomer separation of aliphatic amino acids in standard-sized columns, while miniaturized columns allowed interfacing with an MS-detector.

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Nature of Specific Ligand-Receptor Bonds, in Particular the Antigen-Antibody Bond

Cited by 20 publications

References 52 publications

Measurements of the Forces in Protein Interactions with Atomic Force Microscopy

Measurements of the Forces in Protein Interactions with Atomic Force Microscopy

IgG Dimers in Multidonor-Derived Immunoglobulins: Aspects of Generation and Function

New developments in the production and use of stereoselective antibodies

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