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

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

Research output: Contribution to journalArticlepeer-review

11 Scopus citations

Abstract

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.

Original languageEnglish (US)
Article number163701
JournalApplied Physics Letters
Volume104
Issue number16
DOIs
StatePublished - Apr 21 2014

ASJC Scopus subject areas

  • Physics and Astronomy (miscellaneous)

Fingerprint

Dive into the research topics of 'Label-free, real-time detection of the dynamic processes of protein degradation using oblique-incidence reflectivity difference method'. Together they form a unique fingerprint.

Cite this