Analysis of the binding of bispecific monoclonal antibodies with immobilized antigens (human IgG and horseradish peroxidase) using a resonant mirror biosensor

Dmitriev, D. A.; Massino, Yu. S.; Segal, O.L.; Smirnova, M. B.; Pavlova, Elena; Gurevich, K. G.; Gnedenko, O. V.; Ivanov, Yuriy D.; Kolyaskina, G. I.; Archakov, Alexander I.; Осипов, А. И.; Дмитриев, А. Д.; Egorov, A. M.

doi:10.1016/s0022-1759(01)00558-0

Cited by 28 publications

(9 citation statements)

References 47 publications

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“…The formation of permanent complexes may be considered as a continuation of protein folding, so their surface properties are similar to the protein core or domain interface [10]. The properties of temporary complex interfaces are unique for each interacting pair of proteins and can be considered as analogues of active site of the enzyme [11].…”

Section: Introductionmentioning

confidence: 99%

Protein‐protein interactions as a target for drugs in proteomics

et al. 2003

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Protein-protein interactions play a central role in numerous processes in the cell and are one of the main fields of functional proteomics. This review highlights the methods of bioinformatics and functional proteomics of protein-protein interaction investigation. The structures and properties of contact surfaces, forces involved in protein-protein interactions, kinetic and thermodynamic parameters of these reactions were considered. The properties of protein contact surfaces depend on their functions. The contact surfaces of permanent complexes resemble domain contacts or the protein core and it is reasonable to consider such complex formation as a continuation of protein folding. Characteristics of contact surfaces of temporary protein complexes share some similarities with active sites of enzymes. The contact surfaces of the temporary protein complexes have unique structure and properties and they are more conservative in comparison with active site of enzymes. So they represent prospective targets for a new generation of drugs. During the last decade, numerous investigations were undertaken to find or design small molecules that block protein dimerization or protein(peptide)-receptor interaction, or, on the contrary, to induce protein dimerization.

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Section: Introductionmentioning

confidence: 99%

Protein‐protein interactions as a target for drugs in proteomics

et al. 2003

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“…A majority of the past studies using resonant mirror sensor indicated that this system is suitable for detection of toxins or soluble protein fractions. 5,20 In conclusions, both sensors show promise in detection of low levels of target pathogens in near rea l-time. Early experiments with artificially inoculated or naturally contaminated food samples show promise; however, often there are some inhibitors in food showing reduced signals.…”

Section: Resonant Mirror Immunosensormentioning

confidence: 88%

“…3,11,14,16 Foodborne pathogen detection in food product after processing but before consumption is essent ial to protect consumers from infection or even from fatalities. Sensors that are currently being investigated for their suitability to detect pathogens include impedance-based sensor, cell-based sensor, fiber-optic, 1,6,12,22,23 surface plasmon resonance sensor, 4,5,13,20,21 potentiometric, amperometric, quartz-crystal microbalance, etc. 3,16,21 Many of those sensors are fabricated to perform a specific task, i.e., to detect a specific chemical or biological molecule.…”

Section: Introductionmentioning

confidence: 99%

Optical immunosensors for detection of Listeria monocytogenes and Salmonella enteritidis from food

Bhunia

Geng

Lathrop

et al. 2004

Monitoring Food Safety, Agriculture, and Plant Health

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Listeria monocytogenes and Salmonella are two major foodborne pathogens of significant concern. Two optical evanescent wave immunosensors were evaluated for detection: Antibody-coupled fiber-optic biosensor and a surface plasmon resonant (SPR) immunosensor. In the fiber-optic sensor, polyclonal antibodies for the test organisms were immobilized on polystyrene fiber wave -guides using streptavidin -biotin chemistry. Cyanine 5 -labeled monoclonal antibodies C11E9 (for L. monocytogenes) and SF-11 (for Salmonella Enteritidis) were used to generate a specific fluorescent signal. Signal acquisition was performed by launching a laser-light (635 nm) from an Analyte-2000. This immunosensor was able to detect 10 3 -10 9 cfu/ml of L. monocytogenes or 10 6 -10 9 cfu/ml of Salmonella Enteritidis and the assays were conducted at near real-time with results obtained within one hour of sampling. The assays were specific and showed signal even in the presence of other microorganisms such as E. coli, Enterococcus faecalis or Salmonella Typhimurium. In the SPR system, IAsys instrument (resonant mirror sensor) was used. Monoclonal antibody-C11E9 was directly immobilized onto a carboxylate cuvette. Whole Listeria cells at various concentrations did not yield any signal while surface protein extracts did. Crude protein extracts from L. monocytogenes and L. innocua had average binding responses of around 150 arc sec (0.25 ng/mm 2 ), which was significantly different from L. grayi, L. ivanovii, or L. welshimeri with average responses of <48 arc sec. Both fiber-optic and SPR sensors show promise in near real-time detection of foodborne L. monocytogenes and Salmonella Enteritidis.

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“…Of all biosensor types, particular attention should be paid to noncontact OBs that have found an ever-widening application in biology and medicine [54][55][56][57][58][59][60][61][62][63][64][65][66][67][68][69]. They are used in the real-time analyses of protein -protein interactions including the interactions between antigen/antibody, oligonucleotide/ oligonucleotide, protein/lipid, hormone/receptor and, also, drug/receptor -with the latter interactions being widely used for drug design and drug testing.…”

Section: Obsmentioning

confidence: 99%

Nanotechnologies in proteomics

Ivanov

Govorun

Быков³

et al. 2006

Proteomics

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Progress in proteomic researches is largely determined by development and implementation of new methods for the revelation and identification of proteins in biological material in a wide concentration range (from 10 23 M to single molecules). The most perspective approaches to address this problem involve (i) nanotechnological physicochemical procedures for the separation of multicomponent protein mixtures; among these of particular interest are biospecific nanotechnological procedures for selection of proteins from multicomponent protein mixtures with their subsequent concentration on solid support; (ii) identification and counting of single molecules by use of molecular detectors. The prototypes of biospecific nanotechnological procedures, based on the capture of ligand biomolecules by biomolecules of immobilized ligate and the concentration of the captured ligands on appropriate surfaces, are well known; these are affinity chromatography, magnetic biobeads technology, different biosensor methods, etc. Here, we review the most promising nanotechnological approaches for selection of proteins and kinetic characterization of their complexes based on these biospecific methods with subsequent MS/MS identification of proteins and protein complexes. Two major groups of methods for the analysis and identification of individual molecules and their complexes by use of molecular detectors will be reviewed: scanning probe microscopy (SPM) (including atomic-force microscopy) and cryomassdetector technology.

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Analysis of the binding of bispecific monoclonal antibodies with immobilized antigens (human IgG and horseradish peroxidase) using a resonant mirror biosensor

Cited by 28 publications

References 47 publications

Protein‐protein interactions as a target for drugs in proteomics

Protein‐protein interactions as a target for drugs in proteomics

Optical immunosensors for detection of Listeria monocytogenes and Salmonella enteritidis from food

Nanotechnologies in proteomics

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