Monitoring conformational changes of immobilized RNase A and Lysozyme in reductive unfolding by surface plasmon resonance

Monitoring the Kinetics of the pH-Driven Transition of the Anthrax Toxin Prepore to the Pore by Biolayer Interferometry and Surface Plasmon Resonance

“…The only caveat for monitoring conformational changes during unfolding occurs in instances where proteins interact with the negatively charged CMD matrix due to electrostatic interactions during pH induced unfolding (pH 4 to 10) (5) . When matrix effects are specifically avoided, conformational changes due to unfolding are readily observable (3, 4) . Naturally, protein denaturation changes often generate signals that are much lower than signals observed for protein-protein interactions.…”

A neglected modulator of insulin-degrading enzyme activity and conformation: The pH

“…Large scale protein conformational changes can be observed using surface plasmon resonance (SPR). For example, SPR was previously utilized to observe the conformational changes or unfolding that results from urea-induced unfolding of immobilized luciferase, lysozyme, and RNase proteins [49,50]. However, it has been reported that the potential origins of shifts in the angle of SPR can be numerous and tricky, so, before assigning SPR shifts to pH induced conformational changes, one should take into account all the factors that may affect the properties of the bulk solution, the carboxymethyldextran (CMD) layer and the immobilized biomolecule at the sensor surface.…”

Preliminary Recognition of c-Myc Gene Protein Using an Optical Biosensor with Gold Colloid Nanoparticles Based on Localized Surface Plasmon Resonance

“…In physics, it is well known that in a localized surface plasmon resonance (LSPR), the incident photon frequency is resonant with the collective oscillation of the spatially confined conduction electrons on a noble metal NP, showing its much higher sensitivity increased more than that on a metal surface of a SPR device (Murray, Astilean, and Barnes 2004;Seal et al 2006). In comparison with several reported label-free biosensors based on SPR (Chen 2009;Stepanov et al 2009;Joung et al 2008;Shankaran, Gobi, and Miura 2007;Fu et al 2004) and quartz crystal microbalance (QCM) (Wang et al 2004;Cao et al 2007;Safina, van Lier, and Danielsson 2008;Pedroso et al 2008), the LSPR nanosensor based on NP size and shape could yield ultrasensitive biodetection with extremely simple, small, light, robust, and low-cost instrumentation (Cao et al 2005Takei, Pipper, and Cao 2002). In this article, a novel optical nanobiosensor assembled with Au NPs on an Au surface has been preliminarily constructed for detection of c-Myc gene-related biomolecules based on LSPR phenomena, which will provide valuable information for anticancer predictive and therapeutic strategies.…”

“…Among many advantages of the optical biosensors, sensitivity and real-time detection of biomolecular interactions gave them wide application (Chan and Nie 1998;McFarland and Van Duyne 2003). As one knows, the optical sensor techniques are based on various sensing transduction mechanisms, such as fluorescence (Gong et al 2006Lee et al 2008;Dao et al 2009), chemiluminescence (Chan et al 2002;Ashkenazi, Abu-Rabeah, and Marks 2009), light absorption and scattering (Malinsky et al 2001;Xiang et al 2008), reflectance (Hicks et al 2005;Filik et al 2008), surface plasmon resonance (SPR) (Chen 2009;Stepanov et al 2009;Joung et al 2008), and Raman scattering (Nie and Emory 1997;Zhang et al 2005;Jiang et al 2003;Jeong et al 2009). Biosensing with surface plasmon resonance (SPR) was first established in the early 1980s and quickly became the benchmark technique for label-free detection over the following 30 years (Hoa, Kirk, and Tabrizian 2007;Fan et al 2008;Leung, Shankar, and Mutharasan 2007;Boozer et al 2006;Shankaran, Gobi, and Miura 2007).…”