Quartz Crystal Microbalance for Bioanalytical Applications

ChemInform ◽  
2003 ◽  
Vol 34 (17) ◽  
Author(s):  
A. Janshoff ◽  
C. Steinem
Biosensors ◽  
2020 ◽  
Vol 10 (12) ◽  
pp. 189
Author(s):  
María Calero ◽  
Román Fernández ◽  
Pablo García ◽  
José Vicente García ◽  
María García ◽  
...  

Integrating acoustic wave sensors into lab-on-a-chip (LoC) devices is a well-known challenge. We address this challenge by designing a microfluidic device housing a monolithic array of 24 high-fundamental frequency quartz crystal microbalance with dissipation (HFF-QCMD) sensors. The device features six 6-µL channels of four sensors each for low-volume parallel measurements, a sealing mechanism that provides appropriate pressure control while assuring liquid confinement and maintaining good stability, and provides a mechanical, electrical, and thermal interface with the characterization electronics. We validate the device by measuring the response of the HFF-QCMD sensors to the air-to-liquid transition, for which the robust Kanazawa–Gordon–Mason theory exists, and then by studying the adsorption of model bioanalytes (neutravidin and biotinylated albumin). With these experiments, we show how the effects of the protein–surface interactions propagate within adsorbed protein multilayers, offering essentially new insight into the design of affinity-based bioanalytical sensors.


2019 ◽  
Vol 25 (6) ◽  
pp. 879-884
Author(s):  
Takahiro Sakai ◽  
Hayato Seki ◽  
Shogo Yoshida ◽  
Hayato Hori ◽  
Hisashi Suzuki ◽  
...  

1998 ◽  
Vol 145 (2) ◽  
pp. 492-497 ◽  
Author(s):  
James J. Kelly ◽  
K. M. Anisur Rahman ◽  
Christopher J. Durning ◽  
Alan C. West

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Sin-Cih Sun ◽  
Hung-Wei Huang ◽  
Yi-Ting Lo ◽  
Min-Chieh Chuang ◽  
Yuan-Hao Howard Hsu

AbstractCardiolipin (CL), a crucial component in inner mitochondrial membranes, interacts with cytochrome c (cyt c) to form a peroxidase complex for the catalysis of CL oxidation. Such interaction is pivotal to the mitochondrial regulation of apoptosis and is affected by the redox state of cyt c. In the present study, the redox-dependent interaction of cyt c with CL was investigated through amide hydrogen/deuterium exchange coupled with mass spectrometry (HDXMS) and quartz crystal microbalance with dissipation monitoring (QCM-D). Ferrous cyt c exhibited a more compact conformation compared with its ferric form, which was supported by the lower number of deuterons accumulated and the greater amplitude reduction on dissipation. Upon association with CL, ferrous cyt c resulted in a moderate increase in deuteration, whereas the ferric form caused a drastic increase of deuteration, which indicated that CL-bound ferric cyt c formed an extended conformation. These results were consistent with those of the frequency (f) − dissipation (D) experiments, which revealed that ferric cyt c yielded greater values of |ΔD/Δf| within the first minute. Further fragmentation analysis based on HDXMS indicated that the effect of CL binding was considerably different on ferric and ferrous cyt c in the C-helix and the Loop 9–24. In ferric cyt c, CL binding affected Met80 and destabilized His18 interaction with heme, which was not observed with ferrous cyt c. An interaction model was proposed to explain the aforementioned results.


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