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Detection of mutant p53 using field-effect transistor biosensor

Title
Detection of mutant p53 using field-effect transistor biosensor
Author(s)
Han, Sang HeeKim, Sang KyuPark, KyoungsookYi, So YeonPark, Hye-JungLyu, Hong-KunKim, MoonilChung, Bong Hyun
Issued Date
2010-04-14
Citation
Analytica Chimica Acta, v.665, no.1, pp.79 - 83
Type
Article
Author Keywords
Metal oxide semiconductor field-effect transistorBiosensorp53Mutant p53DNA-binding domain
Keywords
ArticleBindingBiochemistryBiosensing TechniquesBiosensorBIOSENSORSCANCERCELLCHARGEControlled StudyDATABASEDNADNA-BindingDNA-Binding DomainDNA-Protein InteractionDOMAINDrain CurrentFet-Type BiosensorsField-EffectField Effect TransistorField Effect TransistorsGeneGene MutationGenesHUMAN TUMORSMesfet DevicesMetal Oxide Semiconductor Field-Effect TransistorMetal Oxide Semiconductor Field-Effect TransistorsMetallic CompoundsMonitoringMOS-FETMos DevicesMutagenesis, Site-DirectedMutant P53Mutant ProteinMutationP53P53 ProteinPriority JournalProtein BindingProtein DNA InteractionProtein ImmobilizationProtein P53Protein Structure, TertiaryProteinsRecombinant ProteinsSemiconductor AnalyzerSensing LayersSurface Plasmon ResonanceSurface PropertyTransistors, ElectronicTumor Suppressor Protein P53
ISSN
0003-2670
Abstract
We assessed the abilities of wild p53 and mutant p53 proteins to interact with the consensus DNA-binding sequence using a MOSFET biosensor. This is the first report in which mutant p53 has been detected on the basis of DNA-protein interaction using a FET-type biosensor. In an effort to evaluate the performance of this protocol, we constructed the core domain of wild p53 and mutant p53 (R248W), which is DNA-binding-defective. After the immobilization of the cognate DNA to the sensing layer, wild p53 and mutant p53 were applied to the DNA-coated gate surface, and subsequently analyzed using a semiconductor analyzer. As a consequence, a significant up-shift in drain current was noted in response to wild p53, but not mutant p53, thereby indicating that sequence-specific DNA-protein interactions could be successfully monitored using a field-effect-based biosensor. These data also corresponded to the results obtained using surface plasmon resonance (SPR) measurements. Taken together, our results show that a FET-type biosensor might be promising for the monitoring of mutant p53 on the basis of its DNA-binding activity, providing us with very valuable insights into the monitoring for diseases, particularly those associated with DNA-protein binding events. © 2010 Elsevier B.V.
URI
http://hdl.handle.net/20.500.11750/3527
DOI
10.1016/j.aca.2010.03.006
Publisher
Elsevier B.V.
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