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Binding behavior of CRP and anti-CRP antibody analyzed with SPR and AFM measurement

Binding behavior of CRP and anti-CRP antibody analyzed with SPR and AFM measurement
Lee, Soo KeunKim, Hyun ChulCho, Sang JoonJeong, Sang WonJeon, Won Bae
DGIST Authors
Lee, Soo KeunKim, Hyun ChulJeong, Sang WonJeon, Won Bae
Issue Date
Ultramicroscopy, 108(10), 1374-1378
Article Type
Acoustic MicroscopesAFM ImagingAmine GroupsAminesAmplitude ModulationAntibodiesAntibodyAtomic Force MicroscopeAtomic Force MicroscopyBinding BehaviorsBiosensing TechniquesBiosensorBis(N Succinimido) 11,11&aposDithiobis(Undecyl Succinate)C-Reactive ProteinC Reactive ProteinC Reactive Protein AntibodyChlorine CompoundsComparative AnalysisComparative AnatomyCrystallographyExtreme Ultraviolet LithographyGoldGold CompoundsGold MetallurgyGold SurfacesImaging TechniquesMicroscopy, Atomic ForceMineralogyMissile BasesMolecular ImagingMolecular TopologiesN-HydroxysuccinimideN HydroxysuccinimideNanofabricationOrganic CompoundsOutside DiameterPhosphate-Buffered SalinePore DiametersProtein BindingProtein StructureSelf-Assembled MonolayerSelf AssemblySensorSensorsSolution TopologySPR SensorsSuccinic Acid DerivativeSurface Plasmon ResonanceSurface Plasmon Resonance SensorsSynthesisUnclassified DrugX Ray Crystallography
Atomic force microscope (AFM) was exploited to take picture of the molecular topology of C-reactive protein (CRP) in phosphate-buffered saline (PBS) solution. An explicit molecular image of CRP demonstrated a pentagonal structure composed of five subunits. Dimensions of the doughnut-shaped CRP molecule measured by AFM were about 25 nm in outside diameter and 10 nm in central pore diameter, and the height of CRP molecule was about 4 nm which was comparable to the value determined by X-ray crystallography. Bis(N-succinimido)-11,11′-dithiobis (undecyl succinate) (DSNHS) was synthesized for use as a linker for immobilizing anti-CRP antibody (anti-CRP) onto the gold surface of a surface plasmon resonance (SPR) sensor chip. DSNHS formed self-assembled monolayer (SAM) on the gold surface. By use of an AFM tip, a pattern of ditch was engraved within the SAM of DSNHS, and anti-CRP was immobilized on the engraved SAM through replacement of N-hydroxysuccinimide group on the outside surface of DSNHS by the amine group of anti-CRP. Formation of CRP/anti-CRP complex on the gold surface of SPR sensor chip was clearly demonstrated by measuring SPR angle shift. A consecutive series of SAM, SAM/anti-CRP, and SAM/anti-CRP/CRP complexes was generated on a SPR sensor chip, and the changes in depth of the ditch were monitored by taking AFM images of the complexes. Comparative analysis of the depth differences indicates that binding of CRP to anti-CRP occurs in a planar mode. © 2008 Elsevier B.V. All rights reserved.
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