Nano Archive

Resonance localized surface plasmon spectroscopy: Sensing substrate and inhibitor binding to cytochrome P450

Zhao, Jing and Das, Aditi and Schatz, George C. and Sligar, Stephen G. and Van Duyne, Richard P. (2008) Resonance localized surface plasmon spectroscopy: Sensing substrate and inhibitor binding to cytochrome P450. JOURNAL OF PHYSICAL CHEMISTRY C, 112 (34). pp. 13084-13088.

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Official URL: http://dx.doi.org/10.1021/jp801719c

Abstract

A sensing method based on resonance localized surface plasmon spectroscopy was developed for low molecular weight substrate and inhibitor molecules binding to heme proteins. Cytochrome P450 proteins have Soret and Q absorption bands in the visible wavelength region. The coupling between the molecular resonance of P450 and the localized surface plasmon resonance (LSPR) of functionalized silver nanoparticles leads to a highly wavelength-dependent LSPR response. Binding of substrate (e.g., camphor) or inhibitor (e.g., imidazole) molecules to a cytochrome P450 causes the absorption band of cytochrome P450 shift to shorter or longer wavelengths, respectively. By monitoring the localized surface plasmon resonance (LSPR) of the nanosensors, the binding of camphor/imidazole to a nanoparticle whose surface is modified with cytochrome P450 protein leads to a wavelength-dependent blue/red shift in the LSPR. The magnitude of the LSPR shift induced by camphor or imidazole is consistent with the Soret band wavelength shift observed in P450 in solution.

Item Type:Article
Subjects:Analytical Science > Nanotechnology for sensing and actuating
Material Science > Nanochemistry
Material Science > Nanostructured materials
Analytical Science > Beam methods
ID Code:1216
Deposited By:Anuj Seth
Deposited On:16 Dec 2008 11:48
Last Modified:19 Jan 2009 11:48

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