The development of ultrasensitive and rapid approaches to detect tumor markers at very low concentrations even in a physiological environment represents a challenge in nano-medicine. The p53 protein is at the center of the cellular network that protects organisms against the insurgence of tumors, most of which are related to alteration of p53 expression. Therefore p53 is regarded as a valuable prognostic marker whose detection at high sensitivity may considerably contribute to early diagnosis of cancers. In this work we have applied an analytical method based on surface enhanced Raman spectroscopy with high sensitivity and rapidity to improve traditional bioaffinity techniques. The Raman reporter bifunctional linker 4-aminothiophenol (4-ATP) first assembled onto 50 nm gold nanoparticles (Nps) has then been azotated to bind low concentration wild-type and two mutated forms of p53 proteins. The Raman signal enhancement of the resulting p53-(4-ATP-Np) systems has been used to identify the p53 molecules captured on a recognition substrate constituted by the azurin (Az) protein monolayer. Az has shown a strong association for both wild-type and mutated p53 proteins, allowing us to selectively detect these proteins at concentrations as low as 500 IM, in a human serum environment. (C) 2011 Elsevier Inc. All rights reserved.

Domenici, F., Bizzarri, A.r., Cannistraro, S. (2012). Surface-enhanced Raman scattering detection of wild-type and mutant p53 proteins at very low concentration in human serum. ANALYTICAL BIOCHEMISTRY, 421(1), 9-15 [10.1016/j.ab.2011.10.010].

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

Domenici F.
Investigation
;
2012-01-01

Abstract

The development of ultrasensitive and rapid approaches to detect tumor markers at very low concentrations even in a physiological environment represents a challenge in nano-medicine. The p53 protein is at the center of the cellular network that protects organisms against the insurgence of tumors, most of which are related to alteration of p53 expression. Therefore p53 is regarded as a valuable prognostic marker whose detection at high sensitivity may considerably contribute to early diagnosis of cancers. In this work we have applied an analytical method based on surface enhanced Raman spectroscopy with high sensitivity and rapidity to improve traditional bioaffinity techniques. The Raman reporter bifunctional linker 4-aminothiophenol (4-ATP) first assembled onto 50 nm gold nanoparticles (Nps) has then been azotated to bind low concentration wild-type and two mutated forms of p53 proteins. The Raman signal enhancement of the resulting p53-(4-ATP-Np) systems has been used to identify the p53 molecules captured on a recognition substrate constituted by the azurin (Az) protein monolayer. Az has shown a strong association for both wild-type and mutated p53 proteins, allowing us to selectively detect these proteins at concentrations as low as 500 IM, in a human serum environment. (C) 2011 Elsevier Inc. All rights reserved.
2012
Pubblicato
Rilevanza internazionale
Articolo
Esperti anonimi
Settore CHIM/02 - CHIMICA FISICA
English
Raman-SERS; p53; Ultrasensitive detection; Atomic force microscopy; Aniline Compounds; Azurin; Biomarkers, Tumor; Blood Chemical Analysis; Genes, p53; Gold; Humans; Metal Nanoparticles; Mutant Proteins; Neoplasms; Spectrum Analysis, Raman; Sulfhydryl Compounds; Tumor Suppressor Protein p53
Domenici, F., Bizzarri, A.r., Cannistraro, S. (2012). Surface-enhanced Raman scattering detection of wild-type and mutant p53 proteins at very low concentration in human serum. ANALYTICAL BIOCHEMISTRY, 421(1), 9-15 [10.1016/j.ab.2011.10.010].
Domenici, F; Bizzarri, Ar; Cannistraro, S
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/201504
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