Self-Assembly of Perfunctionalized β-Cyclodextrins on a Quartz Crystal Microbalance for Real-Time Chiral Recognition

Langmuir ◽  
2008 ◽  
Vol 24 (16) ◽  
pp. 9118-9124 ◽  
Author(s):  
Changhua Xu ◽  
Siu Choon Ng ◽  
Hardy Sze On Chan
Chirality ◽  
2009 ◽  
pp. NA-NA ◽  
Author(s):  
Miao Li Luo ◽  
Wei Guang Zhang ◽  
Sheng Zhang ◽  
Jun Fan ◽  
Wen Cui Su ◽  
...  

Sensors ◽  
2021 ◽  
Vol 21 (12) ◽  
pp. 4166
Author(s):  
Román Fernández ◽  
María Calero ◽  
Yolanda Jiménez ◽  
Antonio Arnau

Monolithic quartz crystal microbalance (MQCM) has recently emerged as a very promising technology suitable for biosensing applications. These devices consist of an array of miniaturized QCM sensors integrated within the same quartz substrate capable of detecting multiple target analytes simultaneously. Their relevant benefits include high throughput, low cost per sensor unit, low sample/reagent consumption and fast sensing response. Despite the great potential of MQCM, unwanted environmental factors (e.g., temperature, humidity, vibrations, or pressure) and perturbations intrinsic to the sensor setup (e.g., mechanical stress exerted by the measurement cell or electronic noise of the characterization system) can affect sensor stability, masking the signal of interest and degrading the limit of detection (LoD). Here, we present a method based on the discrete wavelet transform (DWT) to improve the stability of the resonance frequency and dissipation signals in real time. The method takes advantage of the similarity among the noise patterns of the resonators integrated in an MQCM device to mitigate disturbing factors that impact on sensor response. Performance of the method is validated by studying the adsorption of proteins (neutravidin and biotinylated albumin) under external controlled factors (temperature and pressure/flow rate) that simulate unwanted disturbances.


Nanoscale ◽  
2019 ◽  
Vol 11 (23) ◽  
pp. 11107-11113 ◽  
Author(s):  
Ye Yang ◽  
Guillaume Poss ◽  
Yini Weng ◽  
Runzhang Qi ◽  
Hanrui Zheng ◽  
...  

We report on a novel screening route to obtain quantitative measures for nanoparticle binding affinities to target analytes.


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