Label-free, real-time detection of the dynamic processes of protein degradation using oblique-incidence reflectivity difference method.

Liu, S; Zhu, J H; He, L P; Dai, J; Lu, H B; Wu, L; Jin, K J; Yang, G Z; Zhu, H

Liu, S; Zhu, J H; He, L P; Dai, J; Lu, H B; Wu, L; Jin, K J; Yang, G Z; Zhu, H.

Afiliación

Liu S; Beijing National Laboratory for Condensed Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190, China.
Zhu JH; CAS Key Laboratory of Genome Sciences and Information, Beijing Institute of Genomics, Chinese Academy of Sciences, Beijing 100101, China.
He LP; Beijing National Laboratory for Condensed Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190, China.
Dai J; Beijing National Laboratory for Condensed Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190, China.
Lu HB; Beijing National Laboratory for Condensed Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190, China.
Wu L; CAS Key Laboratory of Genome Sciences and Information, Beijing Institute of Genomics, Chinese Academy of Sciences, Beijing 100101, China.
Jin KJ; Beijing National Laboratory for Condensed Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190, China.
Yang GZ; Beijing National Laboratory for Condensed Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190, China.
Zhu H; Department of Pharmacology and Molecular Sciences, and The HiT Center, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.

Appl Phys Lett ; 104(16): 163701, 2014 Apr 21.

Article en En | MEDLINE | ID: mdl-24803682

RESUMEN

Based on the requirements for studying the dynamic process of proteinase action substrates in life science, we selected six random proteins including 1L-10, SCGB2A2, CENPQ, GST, HK1, KLHL7, as well as five different concentrations of 1L-10 proteins of 1 mg/ml, 0.5 mg/ml, 0.25 mg/ml, 0.125 mg/ml, and 0.0625 mg/ml, and fabricated two types of substrate protein microarrays, respectively. We detected the dynamic processes of proteins degraded by proteinase K using oblique-incidence reflectivity difference (OIRD) method in a label-free and real-time manner. We obtained the relevant degradation velocities and the degradation time. The experimental results demonstrate that OIRD has the ability to study proteinase action substrates which is out of reach of label methods and is expected to offer opportunities to determine protease-substrate relationships on the systems biology level.

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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Tipo de estudio: Diagnostic_studies / Incidence_studies / Risk_factors_studies Idioma: En Revista: Appl Phys Lett Año: 2014 Tipo del documento: Article País de afiliación: China Pais de publicación: Estados Unidos

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