scholarly journals Quartz Crystal Microbalance With Dissipation Monitoring: A Powerful Method to Predict the in vivo Behavior of Bioengineered Surfaces

2018 ◽  
Vol 6 ◽  
Author(s):  
Chiara Tonda-Turo ◽  
Irene Carmagnola ◽  
Gianluca Ciardelli
Keyword(s):  
Quartz Crystal Microbalance ◽  
Quartz Crystal ◽  
Powerful Method

scholarly journals Protein Adsorption to Titanium and Zirconia Using a Quartz Crystal Microbalance Method

2017 ◽  
Vol 2017 ◽  
pp. 1-8 ◽  
Author(s):  
You Kusakawa ◽  
Eiji Yoshida ◽  
Tohru Hayakawa
Keyword(s):  
Surface Roughness ◽  
Protein Adsorption ◽  
Quartz Crystal Microbalance ◽  
Quartz Crystal ◽  
Adsorption Rate ◽  
Force Microscopy ◽  
Atomic Force ◽  
A Cell ◽  
Addition Amount

Protein adsorption onto titanium (Ti) or zirconia (ZrO2) was evaluated using a 27 MHz quartz crystal microbalance (QCM). As proteins, fibronectin (Fn), a cell adhesive protein, and albumin (Alb), a cell adhesion-inhibiting protein, were evaluated. The Ti and ZrO2 sensors for QCM were characterized by atomic force microscopy and electron probe microanalysis observation, measurement of contact angle against water, and surface roughness. The amounts of Fn and Alb adsorbed onto the Ti and ZrO2 sensors and apparent reaction rate were obtained using QCM measurements. Ti sensor showed greater adsorption of Fn and Alb than the ZrO2 sensor. In addition, amount of Fn adsorbed onto the Ti or ZrO2 sensors was higher than that of Alb. The surface roughness and hydrophilicity of Ti or ZrO2 may influence the adsorption of Fn or Alb. With regard to the adsorption rate, Alb adsorbed more rapidly than Fn onto Ti. Comparing Ti and ZrO2, Alb adsorption rate to Ti was faster than that to ZrO2. Fn adsorption will be effective for cell activities, but Alb adsorption will not. QCM method could simulate in vivo Fn and Alb adsorption to Ti or ZrO2.

Microfluidic Measurements of Drug Dissolution Using a Quartz Crystal Microbalance

2016 ◽  
Author(s):  
Shelly Gulati ◽  
Janpierre A. Bonoan ◽  
Kylee V. Schesser ◽  
Joshua F. Arucan ◽  
Xiaoling Li
Keyword(s):  
Benzoic Acid ◽  
Quartz Crystal Microbalance ◽  
Quartz Crystal ◽  
Rapid Test ◽  
The Body ◽  
Drug Dissolution ◽  
Dissolution Profile ◽  
Dissolution Testing ◽  
Testing Method

This work describes a microfluidic drug dissolution testing method that was developed using a commercial quartz crystal microbalance (QCM) resonator combined with an axial microfluidic flow cell. Dissolution testing is used to obtain temporal dissolution profiles of drugs, which provide information on the bioavailability or the drug’s ability to be completely dissolved and then absorbed and utilized by the body. Feasibility of the QCM dissolution testing method was demonstrated using a sample drug system of thin films of benzoic acid dissolved in water, capturing the drug dissolution profile under different microflow conditions. Our analysis method uses the responses of resonance frequency and resistance of the quartz crystal during dissolution testing to determine the characteristic profiles of benzoic acid dissolved over a range of microflows (10–1000 μL/min). The initial dissolution rates were obtained from the characteristic profiles and found to increase with higher flow rates. This aligns with the expected trend of increased dissolution with higher hydrodynamic forces. The QCM-based microfluidic drug dissolution testing method has advantages over conventional dissolution test methods, including reduced sample sizes, rapid test durations, low resource requirements, and flow conditions that more closely model in vivo conditions.

Interaction of Clear Flavor Emulsions Containing Lemon Essential Oils with Lipid Bilayers via a Quartz Crystal Microbalance

2019 ◽  
Vol 25 (6) ◽  
pp. 879-884
Author(s):  
Takahiro Sakai ◽  
Hayato Seki ◽  
Shogo Yoshida ◽  
Hayato Hori ◽  
Hisashi Suzuki ◽  
...  
Keyword(s):  
Essential Oils ◽  
Lipid Bilayers ◽  
Quartz Crystal Microbalance ◽  
Quartz Crystal

Effect of Current Distribution on Quartz Crystal Microbalance Measurements

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

scholarly journals Unraveling cardiolipin-induced conformational change of cytochrome c through H/D exchange mass spectrometry and quartz crystal microbalance

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Sin-Cih Sun ◽  
Hung-Wei Huang ◽  
Yi-Ting Lo ◽  
Min-Chieh Chuang ◽  
Yuan-Hao Howard Hsu
Keyword(s):  
Mass Spectrometry ◽  
Quartz Crystal Microbalance ◽  
Quartz Crystal ◽  
Interaction Model ◽  
Moderate Increase ◽  
Exchange Mass Spectrometry ◽  
Mitochondrial Regulation ◽  
Crucial Component ◽  
Drastic Increase ◽  
Hydrogen Deuterium

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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