About: AlGaN/GaN high electron mobility transistors for protein

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: AlGaN/GaN high electron mobility transistors for protein–peptide binding affinity study Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	AlGaN/GaN high electron mobility transistors for protein–peptide binding affinity study
Creator	Ren, Fan Chen, Chih-Chen Chyi, Jen-Inn Hsu, Chen-Pin Hsu, Chia-Hsien Hsu, You-Ren Huang, Chih-Cheng Huang, Yu-Fen Lee, Geng-Yen Li, Sheng-Shian Sun, Yuh-Chang Wang, Yu-Lin Yao, Da-Jeng Cheng, Hui-Teng Yeh, J
Source	Elsevier; Medline; PMC
abstract	Abstract Antibody-immobilized AlGaN/GaN high electron mobility transistors (HEMTs) were used to detect a short peptide consisting of 20 amino acids. One-binding-site model and two-binding-site model were used for the analysis of the electrical signals, revealing the number of binding sites on an antibody and the dissociation constants between the antibody and the short peptide. In the binding-site models, the surface coverage ratio of the short peptide on the sensor surface is relevant to the electrical signals resulted from the peptide–antibody binding on the HEMTs. Two binding sites on an antibody were observed and two dissociation constants, 4.404×10−11 M and 1.596×10−9 M, were extracted from the binding-site model through the analysis of the surface coverage ratio of the short peptide on the sensor surface. We have also shown that the conventional method to extract the dissociation constant from the linear regression of curve-fitting with Langmuir isotherm equation may lead to an incorrect information if the receptor has more than one binding site for the ligand. The limit of detection (LOD) of the sensor observed in the experimental result (∼10pM of the short peptide) is very close to the LOD (around 2.7–3.4pM) predicted from the value of the smallest dissociation constants. The sensitivity of the sensor is not only dependent on the transistors, but also highly relies on the affinity of the ligand-receptor pair. The results demonstrate that the AlGaN/GaN HEMTs cannot only be used for biosensors, but also for the biological affinity study.
has issue date	2013-03-15(xsd:dateTime)
bibo:doi	10.1016/j.bios.2012.09.066
bibo:pmid	23102432
has license	els-covid
sha1sum (hex)	ae4541f6e81606b1d8d6aef48cb91c64a93da564
schema:url	https://doi.org/10.1016/j.bios.2012.09.066
resource representing a document's title	AlGaN/GaN high electron mobility transistors for protein–peptide binding affinity study
has PubMed Central identifier	PMC7157921
has PubMed identifier	23102432
schema:publication	Biosensors and Bioelectronics
resource representing a document's body	covid:ae4541f6e81606b1d8d6aef48cb91c64a93da564#body_text
is schema:about of	named entity 'TRANSISTORS' named entity 'VALUE' named entity 'LANGMUIR ISOTHERM EQUATION' named entity '3.4' named entity 'FITTING' named entity 'SENSOR' named entity 'LINEAR REGRESSION' named entity 'SHORT' named entity 'ALGAN' named entity '2.7' named entity 'MORE THAN ONE' named entity 'OBSERVED' named entity 'BINDING-SITE' named entity 'BUT' named entity 'SIGNALS' named entity 'HIGH' named entity 'CONVENTIONAL' named entity 'BIOSENSORS' named entity '404' named entity 'binding' named entity 'revealing' named entity 'biological' named entity 'experimental' named entity 'peptide' named entity 'transistors' named entity 'predicted' named entity 'short' named entity 'GaN' named entity 'high' named entity 'transistors' named entity 'BINDING AFFINITY' named entity 'STUDY' named entity 'SENSITIVITY' named entity 'BIOLOGICAL' named entity 'LIMIT OF DETECTION' named entity 'TO EXTRACT' named entity 'HAVE' named entity 'PEPTIDE BINDING' named entity 'MODELS' named entity 'AFFINITY' named entity 'LOD' named entity 'RATIO' named entity 'STUDY' named entity 'EXTRACTED' named entity 'RECEPTOR' named entity 'RELEVANT' named entity 'ELECTRICAL' named entity 'DEPENDENT' named entity 'LIGAND' named entity 'HIGH' named entity 'MOBILITY' named entity 'ALGAN' named entity 'ELECTRON' named entity 'RESULTS' named entity 'INFORMATION' named entity 'AMINO ACIDS' named entity 'USED' named entity 'ELECTRON' named entity 'VERY CLOSE' named entity 'PAIR' named entity 'SURFACE' named entity 'SMALLEST' named entity 'CLOSE TO' named entity 'TO DETECT' named entity 'COVERAGE' named entity 'ANALYSIS' named entity 'BINDING SITE'

Faceted Search & Find service v1.13.91 as of Mar 24 2020

Alternative Linked Data Documents: Sponger | ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3229 as of Jul 10 2020, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (94 GB total memory)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software