Logo image
Investigation of C-terminal domain of SARS nucleocapsid protein-Duplex DNA interaction using transistors and binding-site models
期刊文章   同儕審查

Investigation of C-terminal domain of SARS nucleocapsid protein-Duplex DNA interaction using transistors and binding-site models

You-Ren Hsu, Yen-Wen Kang, Jung-Ying Fang, Geng-Yen Lee, Jen-Inn Chyi, Chung-Ke Chang, Chen-Pin Hsu, Tai-Huang Huang, Yu-Fen Huang, Yuh-Chang Sun, …
Sensors and Actuators, B: Chemical, 卷.193, 頁碼.334-339
03/2014

摘要

Binding sites Dissociation constants GaN HEMTs SARS Sensors Instrumentation Materials Chemistry Surfaces Coatings and Films Metals and Alloys Electronic Optical and Magnetic Materials Condensed Matter Physics Electrical and Electronic Engineering
AlGaN/GaN high electron mobility transistors (HEMTs) were used to sense the binding between double stranded DNA (dsDNA) and the severe acute respiratory syndrome coronavirus (SARS-CoV) nucleocapsid protein (N protein). The sensing signals were the drain current change of the HEMTs induced by the protein-dsDNA binding. Binding-site models using surface coverage ratios were utilized to analyze the signals from the HEMT-based sensors to extract the dissociation constants and predict the number of binding sites. Two dissociation constants, K D1 = 0.0955 nM, K D2 = 51.23 nM, were obtained by fitting the experimental results into the two-binding-site model. The result shows that this technique is more competitive than isotope-labeling electrophoretic mobility shift assay (EMSA). We demonstrated that AlGaN/GaN HEMTs were highly potential in constructing a semiconductor-based-sensor binding assay to extract the dissociation constants of nucleotide-protein interaction. © 2013 Elsevier B.V.

相關連結

指標

1 檢視次數

詳細資料

Logo image