Surface-enhanced Raman scattering detection of wild-type and mutant p53 proteins at very low concentration in human serum.

作者: Fabio Domenici , Anna Rita Bizzarri , Salvatore Cannistraro

DOI: 10.1016/J.AB.2011.10.010

关键词: Surface-enhanced Raman spectroscopySubstrate (chemistry)LinkerBiophysicsColloidal goldMolecular biologyAzurinMutantRaman spectroscopyWild typeChemistry

摘要: The development of ultrasensitive and rapid approaches to detect tumor markers at very low concentrations even in a physiological environment represents challenge nano-medicine. p53 protein is the center cellular network that protects organisms against insurgence tumors, most which are related alteration expression. Therefore regarded as valuable prognostic marker whose detection high sensitivity may considerably contribute early diagnosis cancers. In this work we have applied an analytical method based on surface enhanced Raman spectroscopy with rapidity improve traditional bioaffinity techniques. reporter bifunctional linker 4-aminothiophenol (4-ATP) first assembled onto 50 nm gold nanoparticles (Nps) has then been azotated bind concentration wild-type two mutated forms proteins. signal enhancement resulting p53-(4-ATP-Np) systems used identify molecules captured recognition substrate constituted by azurin (Az) monolayer. Az shown strong association for both proteins, allowing us selectively these proteins 500 fM, human serum environment.

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