A Calcium-Modulated Plasmonic Switch

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Abstract
A plasmonic switch based on the calcium-induced conformational changes of calmodulin is shown to exhibit reversible wavelength modulations in response to changing calcium concentration. The extinction maximum (λmax) of a localized surface plasmon resonance (LSPR) sensor functionalized with a novel calmodulin construct, cutinase−calmodulin−cutinase (CutCaMCut), reversibly shifts by 2−3 nm. A high-resolution (HR) LSPR spectrometer with a wavelength resolution (3σ) of 1.5 × 10−2 nm was developed to detect these wavelength modulations in real-time, providing information about the dynamics and structure of the protein. The rate of conversion from open (Ca2+-bound) to closed (Ca2+-free) calmodulin is shown to be ∼4-fold faster than the reverse process, with a closing rate of 0.127 s−1 and opening rate of 0.034 s−1. As far as we are aware, this plasmonic switch marks the first use of LSPR spectroscopy to detect reversible conformational changes in an unlabeled protein.