Journal
IET NANOBIOTECHNOLOGY
Volume 8, Issue 1, Pages 10-17Publisher
INST ENGINEERING TECHNOLOGY-IET
DOI: 10.1049/iet-nbt.2013.0031
Keywords
molecular biophysics; dissociation; biochemistry; high electron mobility transistors; aluminium compounds; gallium compounds; III-V semiconductors; wide band gap semiconductors; biosensors; enzymes; drugs; ligand-receptor binding site models; AlGaN-GaN; cost-effective drug developments; biomolecular interaction; human immunodeficiency virus drugs; peptides; human immunodeficiency virus type 1 reverse transcriptase enzymes; antibodies; HEMT; high electron mobility transistors; binding affinity; dissociation constants; transistor-based sensors
Funding
- National Science Council [NSC 99-2218-E-007 -019 -MY2]
- National Tsing Hua University [100N2049E1]
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Ligand-receptor binding site model is used to elucidate the binding affinity between ligands and receptors, with transistor-based sensors. AlGaN/GaN high electron mobility transistors (HEMTs) were immobilised with antibodies and human immunodeficiency virus type 1 reverse transcriptase enzymes to detect peptides and human immunodeficiency virus drugs, respectively. The signals generated by the sensors because of the binding of the ligands to the receptors were fitted into the binding-site models and analysed. The dissociation constants of the ligand-receptor pairs and the number of the binding sites on the receptors were revealed. The results are very consistent with the data reported by the other methods from the literatures. The incorporation of the HEMTs and the binding-site models is demonstrated to be useful for studying the mechanism of the biomolecular interaction and the application for quick and cost-effective drug developments.
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