@article{PacholskiRosencrantzRosencrantzetal.2020,
  author    = {Pacholski, Claudia and Rosencrantz, Sophia and Rosencrantz, Ruben R. and Balderas-Valadez, Ruth Fabiola},
  title     = {Plasmonic biosensors fabricated by galvanic displacement reactions for monitoring biomolecular interactions in real time},
  series = {Analytical and bioanalytical chemistry : a merger of Fresenius' journal of analytical chemistry, Analusis and Quimica analitica},
  volume    = {412},
  journal   = {Analytical and bioanalytical chemistry : a merger of Fresenius' journal of analytical chemistry, Analusis and Quimica analitica},
  number    = {14},
  publisher = {Springer},
  address   = {Heidelberg},
  issn      = {1618-2642},
  doi       = {10.1007/s00216-020-02414-0},
  pages     = {3433 -- 3445},
  year      = {2020},
  abstract  = {Optical sensors are prepared by reduction of gold ions using freshly etched hydride-terminated porous silicon, and their ability to specifically detect binding between protein A/rabbit IgG and asialofetuin/Erythrina cristagalli lectin is studied. The fabrication process is simple, fast, and reproducible, and does not require complicated lab equipment. The resulting nanostructured gold layer on silicon shows an optical response in the visible range based on the excitation of localized surface plasmon resonance. Variations in the refractive index of the surrounding medium result in a color change of the sensor which can be observed by the naked eye. By monitoring the spectral position of the localized surface plasmon resonance using reflectance spectroscopy, a bulk sensitivity of 296 nm +/- 3 nm/RIU is determined. Furthermore, selectivity to target analytes is conferred to the sensor through functionalization of its surface with appropriate capture probes. For this purpose, biomolecules are deposited either by physical adsorption or by covalent coupling. Both strategies are successfully tested, i.e., the optical response of the sensor is dependent on the concentration of respective target analyte in the solution facilitating the determination of equilibrium dissociation constants for protein A/rabbit IgG as well as asialofetuin/Erythrina cristagalli lectin which are in accordance with reported values in literature. These results demonstrate the potential of the developed optical sensor for cost-efficient biosensor applications.},
  language  = {en}
}
@article{RosencrantzVuHoaNguyenParketal.2016,
  author    = {Rosencrantz, Ruben R. and Vu Hoa Nguyen, and Park, Hyunji and Schulte, Christine and B{\"o}ker, Alexander and Schnakenberg, Uwe and Elling, Lothar},
  title     = {Lectin binding studies on a glycopolymer brush flow-through biosensor by localized surface plasmon resonance},
  series = {Analytical and bioanalytical chemistry : a merger of Fresenius' journal of analytical chemistry and Analusis},
  volume    = {408},
  journal   = {Analytical and bioanalytical chemistry : a merger of Fresenius' journal of analytical chemistry and Analusis},
  publisher = {Springer},
  address   = {Heidelberg},
  issn      = {1618-2642},
  doi       = {10.1007/s00216-016-9667-9},
  pages     = {5633 -- 5640},
  year      = {2016},
  abstract  = {A localized surface plasmon resonance biosensor in a flow-through configuration was applied for investigating kinetics of lectin binding to surface-grafted glycopolymer brushes. Polycarbonate filter membranes with pore sizes of 400 nm were coated with a 114-nm thick gold layer and used as substrate for surface-initiated atom-transfer radical polymerization of a glycomonomer. These grafted from glycopolymer brushes were further modified with two subsequent enzymatic reactions on the surface to yield an immobilized trisaccharide presenting brush. Specific binding of lectins including Clostridium difficile toxin A receptor domain to the glycopolymer brush surface could be investigated in a microfluidic setup with flow-through of the analytes and transmission surface plasmon resonance spectroscopy.},
  language  = {en}
}