Dual-polarization interferometry

Short description: Analytical technique that probes molecular layers adsorbed to the surface of a waveguide

Dual-polarization interferometry (DPI) is an analytical technique that probes molecular layers adsorbed to the surface of a waveguide using the evanescent wave of a laser beam. It is used to measure the conformational change in proteins, or other biomolecules, as they function (referred to as the conformation activity relationship).

## Contents

* 1 Instrumentation
* 2 Applications
* 3 References
* 4 Further reading

## Instrumentation

The technique is quantitative and real-time (10 Hz) with a dimensional resolution of 0.01 nm.[1]

Extensions of dual-polarization interferometry also exist, namely multiple pathlength dual-polarization interferometry (MPL-DPI)[2][3][4] and absorption enhanced DPI. In MPL-DPI quantification of both layer thickness and refractive index (density) and therefore mass per unit area can be made for in situ and ex-situ coated films, where normal DPI can only calculate film properties if the interferogram is constantly monitored. Absorption enhanced DPI[5] (AE-DPI) is used to separate the mass of different molecules on the surface, exploiting the absorption of one of the molecular species compared to the other species on the surface.

## Applications

A novel application for dual-polarization interferometry emerged in 2008, where the intensity of light passing through the waveguide is extinguished in the presence of crystal growth. This has allowed the very earliest stages in protein crystal nucleation to be monitored.[6] Later versions of dual-polarization interferometers also have the capability to quantify the order and disruption in birefringent thin films.[7] This has been used, for example, to study the formation of lipid bilayers and their interaction with membrane proteins.[8][9]

## References

1. ↑ Swann, MJ; Freeman, NJ; Cross, GH (2007). "Dual Polarization Interferometry: A Real-Time Optical Technique for Measuring (Bio)Molecular Orientation, Structure and Function at the Solid/Liquid Interface". in Marks, R.S.. Handbook of Biosensors and Biochips. 1. John Wiley & Sons. Pt. 4, Ch. 33, pp. 549–568. ISBN 978-0-470-01905-4.
2. ↑ Coffey, Paul D.; Swann, Marcus J.; Waigh, Thomas A.; Schedin, Fred; Lu, Jian R. (22 June 2009). "Multiple path length dual polarization interferometry". Optics Express 17 (13): 10959. doi:10.1364/OE.17.010959.
3. ↑ Coffey, Paul. "Interfacial Measurements of Colloidal and Bio-colloidal Systems in Real-Time". https://research.manchester.ac.uk/en/studentTheses/interfacial-measurements-of-colloidal-and-bio-colloidal-systems-i.
4. ↑ Delivopoulos, Evangelos; Ouberai, Myriam M.; Coffey, Paul D.; Swann, Marcus J.; Shakesheff, Kevin M.; Welland, Mark E. (February 2015). "Serum protein layers on parylene-C and silicon oxide: Effect on cell adhesion". Colloids and Surfaces B: Biointerfaces 126: 169–177. doi:10.1016/j.colsurfb.2014.12.020.
5. ↑ Coffey, Paul David; Swann, Marcus Jack; Waigh, Thomas Andrew; Mu, Qingshan; Lu, Jian Ren (2013). "The structure and mass of heterogeneous thin films measured with dual polarization interferometry and ellipsometry". RSC Advances 3 (10): 3316. doi:10.1039/C2RA22911K.
6. ↑ Boudjemline, A; Clarke, DT; Freeman, NJ; Nicholson, JM; Jones, GR (2008). "Early stages of protein crystallization as revealed by emerging optical waveguide technology". Journal of Applied Crystallography 41 (3): 523. doi:10.1107/S0021889808005098.
7. ↑ Mashaghi, A; Swann, M; Popplewell, J; Textor, M; Reimhult, E (2008). "Optical Anisotropy of Supported Lipid Structures Probed by Waveguide Spectroscopy and Its Application to Study of Supported Lipid Bilayer Formation Kinetics". Analytical Chemistry 80 (10): 3666–76. doi:10.1021/ac800027s. PMID 18422336.
8. ↑ Sanghera, N; Swann, MJ; Ronan, G; Pinheiro, TJ (2009). "Insight into early events in the aggregation of the prion protein on lipid membranes". Biochimica et Biophysica Acta (BBA) - Biomembranes 1788 (10): 2245–51. doi:10.1016/j.bbamem.2009.08.005. PMID 19703409.
9. ↑ Lee, TH; Heng, C; Swann, MJ; Gehman, JD; Separovic, F; Aguilar, MI (2010). "Real-time quantitative analysis of lipid disordering by aurein 1.2 during membrane adsorption, destabilisation and lysis". Biochimica et Biophysica Acta (BBA) - Biomembranes 1798 (10): 1977–86. doi:10.1016/j.bbamem.2010.06.023. PMID 20599687.

## Further reading

* Cross, GH; Ren, Y; Freeman, NJ (1999). "Young's fringes from vertically integrated slab waveguides: Applications to humidity sensing". Journal of Applied Physics 86 (11): 6483. doi:10.1063/1.371712. Bibcode: 1999JAP....86.6483C. http://dro.dur.ac.uk/16118/1/16118.pdf.
* Cross, G (2003). "A new quantitative optical biosensor for protein characterisation". Biosensors and Bioelectronics 19 (4): 383–90. doi:10.1016/S0956-5663(03)00203-3. PMID 14615097.
* Freeman, NJ; Peel, LL; Swann, MJ; Cross, GH; Reeves, A; Brand, S; Lu, JR (2004). "Real time, high resolution studies of protein adsorption and structure at the solid–liquid interface using dual polarization interferometry". Journal of Physics 16 (26): S2493–S2496. doi:10.1088/0953-8984/16/26/023. Bibcode: 2004JPCM...16S2493F.
* Khan, TR; Grandin, HM; Mashaghi, A; Textor, M; Reimhult, E; Reviakine, I (2008). "Lipid redistribution in phosphatidylserine-containing vesicles adsorbing on titania.". Biointerphases 3 (2): FA90. doi:10.1116/1.2912098. PMID 20408675.

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Spectroscopy

Vibrational|

* FT-IR
* Raman
* Resonance Raman
* Rotational
* Rotational–vibrational
* Vibrational
* Vibrational circular dichroism

UV–Vis–NIR|

* Ultraviolet–visible
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X-ray and
photoelectron|

* Energy-dispersive X-ray spectroscopy
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* EXAFS

Nucleon|

* Gamma
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Radiowave|

* NMR
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Others|

* Acoustic resonance spectroscopy
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* Circular dichroism spectroscopy
* Coherent anti-Stokes Raman spectroscopy
* Cold vapour atomic fluorescence spectroscopy
* Conversion electron Mössbauer spectroscopy
* Correlation spectroscopy
* Deep-level transient spectroscopy
* Dual-polarization interferometry
* Electron phenomenological spectroscopy
* EPR spectroscopy
* Force spectroscopy
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Protein structural analysis

High resolution|

* Cryo-electron microscopy
* X-ray crystallography
* NMR
* Electron crystallography
* EPR

Medium resolution|

* Fiber diffraction
* Mass spectrometry
* SAXS

Spectroscopic|

* NMR
* Circular dichroism
* Dual-polarization interferometry
* Absorbance
* Fluorescence
* Fluorescence anisotropy

Translational Diffusion|

* Analytical ultracentrifugation
* Size exclusion chromatography
* Light scattering
* NMR

Rotational Diffusion|

* Fluorescence anisotropy
* Flow birefringence
* Dielectric relaxation
* NMR

Chemical|

* Hydrogen-deuterium exchange
* Site-directed mutagenesis
* Chemical modification

Thermodynamic|

* Equilibrium unfolding

Computational|

* Protein structure prediction
* Molecular docking

←Tertiary structure

Quaternary structure→

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