Molecular Recognition in the P450cam Monooxygenase System: Direct Monitoring of Protein–Protein Interactions by Using Optical Biosensor

Ivanov, Yuri D.; Kanaeva, Irina P.; Karuzina, I I; Archakov, Alexander I.; Hoa, Gaston Hui Bon; Sligar, Stephen G.

doi:10.1006/abbi.2001.2405

Cited by 24 publications

(29 citation statements)

References 25 publications

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“…The mere revelation of a complex -without measuring its tightness, specificity and functional activity -is apparently insufficient for its characterization and estimation of its productivity/nonproductivity. This fact, which is well known in enzymology, has found additional confirmation in our studies [59][60]. It was also found that OBs are capable of monitoring in real time the processes of complex formation and decay not only in binary but also in multicomponent complexes.…”

Section: Biomolecular Analysis (Bia) Of Complex Formation By Use Of Osupporting

confidence: 88%

“…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%

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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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Section: Biomolecular Analysis (Bia) Of Complex Formation By Use Of Osupporting

confidence: 88%

Section: Obsmentioning

confidence: 99%

Nanotechnologies in proteomics

Ivanov

Govorun

Быков³

et al. 2006

Proteomics

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“…In this case k 2 must be larger than k 22 and this shifts the reaction to the right. When conformational changes are faster (in comparison to intermediate complex dissociation, i.e.…”

Section: Thermodynamics and Kinetics Of Protein-protein Interactionsmentioning

confidence: 99%

“…Electrostatic forces are the other significant forces involved in protein-protein interactions [21][22][23][24]. The charge density varies from 0-12 charged groups per interface surface [25].…”

Section: Protein-protein Contacts: Structure Composition and Forcesmentioning

confidence: 99%

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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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Atomic force microscopy detection of molecular complexes in multiprotein P450cam containing monooxygenase system

Kuznetsov

Ivanov

Быков³

et al. 2002

Proteomics

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The application of atomic force microscopy (AFM) technique in proteomic research, identification and visualization of individual molecules and molecular complexes within the P450cam containing monooxygenase system was demonstrated. The method distinguishes between the binary protein complexes and appropriate monomeric proteins and, also, between the binary and ternary complexes. The AFM images of the components of a cytochrome P450cam containing monooxygenase system - cytochrome P450cam (P450cam), putidaredoxin (Pd) and putidaredoxin reductase (PdR) - were obtained on a mica support. The molecules of P450cam, Pd and PdR were found to have typical heights of 2.6 +/- 0.3 nm, 2.0 +/- 0.3 and 2.8 +/- 0.3 nm, respectively. The measured heights of the binary Pd/PdR and P450cam/PdR complexes were 4.9 +/- 0.3 nm and 5.1 +/- 0.3 nm, respectively. The binary P450cam/Pd complexes were found to have a typical height of about (3.9 / 5.7 nm) and the ternary PdR/Pd/P450cam complexes, a typical height of about 9.1 +/- 0.3 nm.

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Molecular Recognition in the P450cam Monooxygenase System: Direct Monitoring of Protein–Protein Interactions by Using Optical Biosensor

Cited by 24 publications

References 25 publications

Nanotechnologies in proteomics

Nanotechnologies in proteomics

Protein‐protein interactions as a target for drugs in proteomics

Atomic force microscopy detection of molecular complexes in multiprotein P450cam containing monooxygenase system

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