Dual-Polarization Interferometry
From Handwiki
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).
Instrumentation
The technique is quantitative and real-time (10 Hz) with a dimensional resolution of 0.01 nm.[1]
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.[2] Later versions of dual-polarization interferometers also have the capability to quantify the order and disruption in birefringent thin films.[3] This has been used, for example, to study the formation of lipid bilayers and their interaction with membrane proteins.[4][5]
References
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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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Categories: [Biosensors] [Interferometry] [Protein methods] [Polyelectrolytes] [Scientific instruments] [Scientific equipment]
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