Surface-enhanced Raman scattering detection of wild-type and mutant p53 proteins at very low concentration in human serum.
Anal Biochem
; 421(1): 9-15, 2012 Feb 01.
Article
em En
| MEDLINE
| ID: mdl-22056410
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 fM, in a human serum environment.
Texto completo:
1
Bases de dados:
MEDLINE
Assunto principal:
Análise Espectral Raman
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Proteína Supressora de Tumor p53
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Proteínas Mutantes
Tipo de estudo:
Diagnostic_studies
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Prognostic_studies
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Screening_studies
Limite:
Humans
Idioma:
En
Revista:
Anal Biochem
Ano de publicação:
2012
Tipo de documento:
Article
País de afiliação:
Itália