Hemagglutinin (HA) is the main surface glycoprotein of the influenza A virus. The H9N2 subtype influenza A virus is recognized as the most possible pandemic strain as it has crossed the species barrier, infecting swine and humans. We use terahertz spectroscopy to study the hydration shell formation around H9 subtype influenza A virus's HA protein (H9 HA) as well as the detection of antigen binding of H9 HA with the broadly neutralizing monoclonal antibody. We observe a remarkable concentration dependent nonlinear response of the H9 HA, which reveals the formation process of the hydration shell around H9 HA molecules. Furthermore, we show that terahertz dielectric properties of the H9 HA are strongly affected by the presence of the monoclonal antibody F10 and that the terahertz dielectric loss tangent can be used to detect the antibody binding at lower concentrations than the standard ELISA test.
An all-fiber glucose sensor is proposed and demonstrated based on a helical intermediate-period fiber grating (HIPFG) produced by using a hydrogen/oxygen flame heating method. The HIPFG, with a grating length of 1.7 cm and a period of 35 μm, presents four sets of double dips with low insertion losses and strong coupling strengths in the transmission spectrum. The HIPFG possesses an averaged refractive index (RI) sensitivity of 213.6 nm/RIU nm/RIU in the RI range of 1.33–1.36 and a highest RI sensitivity of 472 nm/RIU at RI of 1.395. In addition, the HIPFG is demonstrated with a low-temperature sensitivity of 3.67 pm/°C, which promises a self-temperature compensation in glucose detection. In the glucose-sensing test, the HIPFG sensor manifests a detection sensitivity of 0.026 nm/(mg/mL) and a limit of detection (LOD) of 1 mg/mL. Moreover, the HIPFG sensor exhibits good stability in 2 h, indicating its capacity for long-time detection. The properties of easy fabrication, high flexibility, insensitivity to temperature, and good stability of the proposed HIPFG endow it with a promising potential for long-term and compact biosensors.
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