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Andreas B. Dahlin

Researcher at Chalmers University of Technology

Publications -  83
Citations -  4171

Andreas B. Dahlin is an academic researcher from Chalmers University of Technology. The author has contributed to research in topics: Surface plasmon resonance & Plasmon. The author has an hindex of 32, co-authored 72 publications receiving 3497 citations. Previous affiliations of Andreas B. Dahlin include Lund University & École Polytechnique Fédérale de Lausanne.

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Improving the instrumental resolution of sensors based on localized surface plasmon resonance.

TL;DR: Generic data analysis algorithms and a simple experimental setup are presented that provide a S/N upon protein binding that is comparable to that of state-of-the art SPR systems and the importance of utilizing changes in both peak position and magnitude is highlighted.
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Label-Free Plasmonic Detection of Biomolecular Binding by a Single Gold Nanorod

TL;DR: Binding of streptavidin at 1 nM concentration induces a mean resonant wavelength shift of 0.59 nm suggesting that the current optical setup is able to reliably measure wavelength shifts as small as 0.3 nm, which is close to the limit of detection of the system.
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Localized surface plasmon resonance sensing of lipid-membrane-mediated biorecognition events.

TL;DR: The hole-induced localization of the LSPR field to the voids of the holes is demonstrated to provide an extension of theLSPR sensing concept to studies of reactions confined exclusively to SPB-patches supported on SiO2, and the possibility of performing label-free studies of lipid-membrane-mediated reaction kinetics is emphasized.
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Plasmonic sensing characteristics of single nanometric holes.

TL;DR: It is established that the plasmon excitations of single and short-range ordered 60 nm holes exhibit similar E-field decay lengths delta approximately 10-20 nm and that a single hole can be used to resolve the successive adsorption of a protein and its interaction partner (neutravidin).
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Nanoplasmonic Sensor Detects Preferential Binding of IRSp53 to Negative Membrane Curvature.

TL;DR: This work shows the first example of analyzing preferential binding of an average-sized and biologically important protein to negative membrane curvature in a label-free manner and in real-time, illustrating a unique application for nanoplasmonic sensors.