Quartz crystal microbalances for quantitative biosensing and characterizing protein multilayers

Rickert, Jan; Brecht, Andreas; Göpel, Wolfgang

doi:10.1016/s0956-5663(96)00077-2

Cited by 103 publications

(63 citation statements)

References 19 publications

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“…In the ideal case, the mass-frequency relationship is described by the Sauerbrey equation. 8 After the gold surface of the QCM electrode is cleaned with piranha solution, the SAM of octadecanethiol is prepared for the adsorption of protein.…”

Section: Methodsmentioning

confidence: 99%

QCM Study of β-Casein Adsorption on the Hydrophobic Surface: Effect of Ionic Strength and Cations

2004

Bulletin of the Korean Chemical Society

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The adsorption kinetics of β-casein on a hydrophobic surface has been studied by means of the quartz crystal microbalance (QCM). The self assembled monolayer of 1-octadecanethiol on a gold coated quartz crystal was used as a hydrophobic surface for adsorption. The adsorption kinetics was monitored in different solution conditions. Formation of monolayer is observed in most cases. At high concentration of protein, micelle formation which is interrupted by high ionic strength of solution is observed. Casein binding cations such as Ca 2+ , Ba 2+ and Al 3+ increase the hydrophobicity of the protein and the multiple layer adsorption occurs. The strong and weak points of the QCM method in the study of protein adsorption are discussed.

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Section: Methodsmentioning

confidence: 99%

QCM Study of β-Casein Adsorption on the Hydrophobic Surface: Effect of Ionic Strength and Cations

2004

Bulletin of the Korean Chemical Society

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“…The instrument was built by following a resonant circuit realized for the same purpose (Facci et al, 1993). Instrument calibration was done by drop casting of incremental amounts of standard Bovine Serum Albumine (BSA) onto the electrodes of crystal quartz resonators (Rickert et al, 1997). The single 5 MHz QCM crystals (catalogue code 151247-5) were purchased by ICM (International Crystal Manufacturing Co., Oklahoma City, USA).…”

Section: Qcm Mass Measurementsmentioning

confidence: 99%

New insights for using self-assembly materials to improve the detection stability in label-free DNA-chip and immuno-sensors

Carrara¹,

Benini²,

Bhalla³

et al. 2009

Biosensors and Bioelectronics

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a b s t r a c tThis paper examines reliable advancements in low-cost DNA-and immuno-chips. Capacitance detection was successfully chosen to develop label-free bio-chips. Probe immobilization was rigorously investigated in order to obtain reliable capacitance measurements. Protein probes immobilized by using usual alkanethiols or thiolated ssDNA probes directly immobilized on gold do not allow sufficient stable capacitance measurements. New alkanethiols improved with ethylene-glycol function are shown in this paper to be more suitable materials for capacitive bio-chip development. Atomic Force Microscopy, Quartz Crystal Microbalance, and Capacitance Measurements were used to demonstrate that ethylene-glycol alkanethiols allow high time stability, smaller errors in detection, and improved ideal behaviour of the sensing surfaces. Measured capacitance is in the range of 8-11 nF/mm 2 for antibody layers and close to 6 nF/mm 2 for DNA probes. It is in the range of 10-12 nF/mm 2 and of 4-6 nF/mm 2 for antigen and DNA detection, respectively. The percentage error in detection is highly improved and it is in the range of 11-37% and of 0,23-0,82% for antigen and DNA, respectively. The reproducibility is also improved and it is close to 0,44% for single spot measurements on ethylene-glycol alkanethiols. A molecular theory attributing these improvements to water molecules strongly coordinated by ethylene-glycol functional groups and to solution ions not entering into probe films is finally proposed.

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“…Concentration-dependent measurements of the frequency shift together with the assumption of a linear relationship between frequency shift and mass load allow the determination of binding and rate constants of protein and peptide adsorption [49,60,62,[69][70][71]. Moreover, the QCM method has been evolved as a routine technique to control the quality of multilayers prepared by the Langmuir-Blodgett technique [72] or self-organization processes [68,[73][74][75][76][77][78][79][80].…”

Section: Adsorption Of Proteins At Functionalized Surfacesmentioning

confidence: 99%

Quartz Crystal Microbalance for Bioanalytical Applications

Janshoff

Steinem

2001

Sensors Update

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The quartz crystal microbalance (QCM) was first introduced as a mass sensor in gas phase and in vacuum. Since oscillator circuits capable of exciting shear vibrations of quartz resonators under liquid load have been developed, the QCM became accepted as a new powerful technique to monitor adsorption processes at solid/liquid interfaces in chemical and biological research rendering the method an attractive low‐cost alternative for bioanalytic applications. In the last decade, adsorption of biomolecules on functionalized surfaces turned out to be one of the paramount applications of piezoelectric transducers comprising the interaction of DNA and RNA with complementary strands, specific recognition of protein‐ligands by immobilized receptors, the detection of virus capsids, bacteria, mammalian cells and last but not least the development of complete immunosensors. Piezoelectric transducers allow a label‐free detection of molecules; they are more than mere mass sensors since the sensor response is also influenced by interfacial phenomena, viscoelastic properties of the adhered biomaterial, surface charges of adsorbed molecules and surface roughness. These new insights have recently been used to investigate the adhesion of cells, liposomes and proteins onto surfaces allowing to determine morphological changes of cells as a response to pharmacological substances and changes in the water content of biopolymers in situ. However, future will show whether the quartz crystal microbalance will assert itself against established label‐free sensor devices like surface plasmon resonance spectroscopy and interferometry.

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Quartz crystal microbalances for quantitative biosensing and characterizing protein multilayers

Cited by 103 publications

References 19 publications

QCM Study of β-Casein Adsorption on the Hydrophobic Surface: Effect of Ionic Strength and Cations

QCM Study of β-Casein Adsorption on the Hydrophobic Surface: Effect of Ionic Strength and Cations

New insights for using self-assembly materials to improve the detection stability in label-free DNA-chip and immuno-sensors

Quartz Crystal Microbalance for Bioanalytical Applications

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