Microfluidic devices for terahertz spectroscopy of biomolecules

George, Paul A.; Hui, Wallace; Rana, Farhan; Hawkins, Benjamin G.; Smith, A. Ezekiel; Kirby, Brian J.

doi:10.1364/oe.16.001577

Cited by 116 publications

(59 citation statements)

References 13 publications

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“…For example, BSA solution in water at 0.1% w/w concentration was shown clearly to have higher absorption compared to water in the 2-2.5 THz spectral domain 3 (as judged by the higher imaginary part of the dielectric constant), while the absorption of BSA in 50 mM phosphate buffer at 101 mg/ml was shown to have less absorption than the buffer by approximately 8% over the frequency domain from 0.5 to 2.5 THz. 34 The BSA concentration in the later study is 100 times higher, and the buffer is also different. Importantly, in this frequency domain, the influence of the intermolecular stretching mode in water, centered at 5.3 THz, has to be considered.…”

Section: Introductionmentioning

confidence: 75%

Sub-terahertz spectroscopy reveals that proteins influence the properties of water at greater distances than previously detected

Sushko¹,

Dubrovka²,

Donnan³

2015

The Journal of Chemical Physics

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Erratum: "Sub-terahertz spectroscopy reveals that proteins influence the properties of water at greater distances than previously detected" [J. Chem. Phys. 142, 055101 (2015) The initial purpose of the study is to systematically investigate the solvation properties of different proteins in water solution by terahertz (THz) radiation absorption. Transmission measurements of protein water solutions have been performed using a vector network analyser-driven quasi-optical bench covering the WR-3 waveguide band (0.220-0.325 THz). The following proteins, ranging from low to high molecular weight, were chosen for this study: lysozyme, myoglobin, and bovine serum albumin (BSA). Absorption properties of solutions were studied at different concentrations of proteins ranging from 2 to 100 mg/ml. The concentration-dependent absorption of protein molecules was determined by treating the solution as a two-component model first; then, based on protein absorptivity, the extent of the hydration shell is estimated. Protein molecules are shown to possess a concentration-dependent absorptivity in water solutions. Absorption curves of all three proteins sharply peak towards a dilution-limit that is attributed to the enhanced flexibility of protein and amino acid side chains. An alternative approach to the determination of hydration shell thickness is thereby suggested, based on protein absorptivity. The proposed approach is independent of the absorption of the hydration shell. The derived estimate of hydration shell thickness for each protein supports previous findings that protein-water interaction dynamics extends beyond 2-3 water solvation-layers as predicted by molecular dynamics simulations and other techniques such as NMR, X-ray scattering, and neutron scattering. According to our estimations, the radius of the dynamic hydration shell is 16, 19, and 25 Å, respectively, for lysozyme, myoglobin, and BSA proteins and correlates with the dipole moment of the protein. It is also seen that THz radiation can serve as an initial estimate of the protein hydrophobicity. C 2015 Author(s). All article content, except where otherwise noted, is licensed under a Creative Commons Attribution 3.0 Unported License. [http://dx

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Section: Introductionmentioning

confidence: 75%

Sub-terahertz spectroscopy reveals that proteins influence the properties of water at greater distances than previously detected

Sushko¹,

Dubrovka²,

Donnan³

2015

The Journal of Chemical Physics

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“…Low THz-loss polymers such as Zeonor 1020R have been used to create suitable devices. 4 The use of plasma polymerised tetramethyldisiloxane is another possible emerging candidate for a polymer solution; 5 however, more detailed work still needs to be undertaken into the THz absorption properties of the material. Silicon-glass microfluidic devices have been demonstrated in the past, 6 though they are unsuitable for THz frequencies due to the scattering effects induced by the glass.…”

Section: Microfluidics For Thz Frequenciesmentioning

confidence: 99%

Silicon based microfluidic cell for terahertz frequencies

Baragwanath

Swift

Dai

et al. 2010

Journal of Applied Physics

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We present a detailed analysis of the design, fabrication and testing of a silicon based, microfluidic cell, for transmission terahertz time-domain spectroscopy. The sensitivity of the device is tested through a range of experiments involving primary alcohol/water mixtures. The dielectric properties of these solutions are subsequently extracted using a Nelder–Mead search algorithm, and are in good agreement with literature values obtained via alternative techniques. Quantities in the order of 2 μmol can be easily distinguished for primary alcohols in solution, even with the subwavelength optical path lengths used. A further display of the device sensitivity is shown through the analysis of commercial whiskeys, where there are clear, detectable differences between samples. Slight absorption variations were identified between samples of the same commercial brand, owing to a 2.5% difference in their alcoholic content. Results from data taken on subsequent days after system realignment are also presented, confirming the robustness of the technique, and the data extraction algorithm used. One final experiment, showing the possible use of this device to analyze aqueous biological samples is detailed; where biotin, a molecule known for its specific terahertz absorptions, is analyzed in solution. The device sensitivity is once again displayed, where quantities of 3 nmol can be clearly detected between samples.

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“…Consequently, THz frequencies bring information concerning radicals, biomolecules but also concerning conformational states of proteins [5,6]. Today, lot of biological studies concern protein-protein or protein-cell real-time interactions [7,8]. THz microfluidic microsystems should be a useful tool to get sensitive and reproducible measurements in this way.…”

Section: Introductionmentioning

confidence: 99%

Terahertz Spiral Planar Goubau Line Rejectors for Biological Characterization

Treizebré¹,

Hofman²,

Bocquet³

2010

PIER M

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Abstract-Terahertz spectroscopy brings precious complementary information in life science by probing directly low energy bindings inside matter. This property has been demonstrated on dehydrated substances, and interesting results are obtained on liquid solutions. The next step is the characterization of living cells.We have successfully integrated THz passive circuits inside Biological MicroElectroMechanical Systems (BioMEMS). They are based on metallic wires called Planar Goubau Line (PGL). We demonstrate that high THz measurement sensitivity can be reached with new design based on spirals. But we show that the principal interest of this design is its high spatial resolution below the wavelength size compatible with living cell investigation.

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Microfluidic devices for terahertz spectroscopy of biomolecules

Cited by 116 publications

References 13 publications

Sub-terahertz spectroscopy reveals that proteins influence the properties of water at greater distances than previously detected

Sub-terahertz spectroscopy reveals that proteins influence the properties of water at greater distances than previously detected

Silicon based microfluidic cell for terahertz frequencies

Terahertz Spiral Planar Goubau Line Rejectors for Biological Characterization

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