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@article{Fattinger2020,
title = {Focal Molography – an optical method for label-free detection of biomolecular interactions},
author = {Fattinger, Christof; Frutiger, Andreas},
url = {https://www.sps.ch/fileadmin/articles-pdf/2020/Mitteilungen_Progress_77.pdf},
year = {2020},
date = {2020-10-01},
journal = {Progress in Physics},
volume = {62},
number = {77},
abstract = {Focal molography is a new method for label-free molecular interaction analysis in crude samples. In contrast to refractometric optical sensors, focal molography is insensitive to nonspecific molecular interactions. This unique property is achieved with a special 2D nanopattern of molecular binding sites on a chip, termed mologram. A mologram is designed such that molecules bound to it diffract light constructively into a focal spot. The intensity of the focused light is measured to quantify the amount of bound molecules. In biological samples, highly abundant off-target molecules readily adsorb to the surface of the sensor. Yet, this process is completely random and the off-target molecules do not bind to the ordered binding sites of the mologram. Thus, their scattering is uniform in all spatial directions and therefore they hardly contribute to the measured light intensity in the narrow solid angle of the focal spot.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}

@article{Reichmuth2020,
title = {Quantification of Molecular Interactions in Living Cells in Real Time using a Membrane Protein Nanopattern},
author = {Andreas Michael Reichmuth and Mirjam Zimmermann and Florian Wilhelm and Andreas Frutiger and Yves Blickenstorfer and Christof Fattinger and Maria Waldhoer and János Vörös},
doi = {10.1021/acs.analchem.0c00987},
issn = {0003-2700},
year = {2020},
date = {2020-01-01},
journal = {Analytical Chemistry},
abstract = {Molecular processes within cells have traditionally been studied with biochemical methods due to their high degree of specificity and ease of use. In recent years, cell-based assays have gained more and more popularity since they facilitate the extraction of mode of action, phenotypic, and toxicity information. However, to provide specificity, cellular assays rely heavily on biomolecular labels and tags while label-free cell-based assays only offer holistic information about a bulk property of the investigated cells. Here, we introduce a cell-based assay for protein–protein interaction analysis. We achieve specificity by spatially ordering a membrane protein of interest into a coherent pattern of fully functional membrane proteins on the surface of an optical sensor. Thereby, molecular interactions with the coherently ordered membrane proteins become visible in real time, while nonspecific interactions and holistic changes within the living cell remain invisible. Due to its unbiased nature, this new cell-based detection method presents itself as an invaluable tool for cell signaling research and drug discovery.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}

@article{Frutiger2019,
title = {Principles for Sensitive and Robust Biomolecular Interaction Analysis: The Limits of Detection and Resolution of Diffraction-Limited Focal Molography},
author = {Andreas Frutiger and Yves Blickenstorfer and Silvio Bischof and Csaba Forró and Matthias Lauer and Volker Gatterdam and Christof Fattinger and János Vörös},
doi = {10.1103/physrevapplied.11.014056},
year = {2019},
date = {2019-01-28},
journal = {Physical Review Applied},
volume = {11},
number = {1},
pages = {014056},
abstract = {Label-free biosensors enable the monitoring of biomolecular interactions in real time, which is key to the analysis of the binding characteristics of biomolecules. While refractometric optical biosensors such as surface plasmon resonance (SPR) are sensitive and well-established, they are susceptible to any change of the refractive index in the sensing volume caused by minute variations in composition of the sample buffer, temperature drifts, and most importantly nonspecific binding to the sensor surface in complex fluids such as blood. The limitations arise because refractometric sensors measure the refractive index of the entire sensing volume. Conversely, diffractometric biosensors–for example, focal molography–only detect the diffracted light from a coherent assembly of analyte molecules. Thus any refractive index distribution that is noncoherent with respect to this molecular assembly does not add to the coherent signal. This makes diffractometric biosensors inherently robust and enables sensitive measurements without reference channels or temperature stabilization. The coherent assembly is generated by selective binding of the analyte molecules to a synthetic binding pattern–the mologram. Focal molography has been introduced theoretically [C. Fattinger, Phys. Rev. X 4, 031024 (2014)] and verified experimentally [V. Gatterdam, A. Frutiger, K.-P. Stengele, D. Heindl, T. Lübbes, J. Vörös, and C. Fattinger, Nat. Nanotechnol. 12, 1089 (2017)] in previous papers. However, further understanding of the underlying physics and a diffraction-limited readout is needed to unveil its full potential. This paper introduces refined theoretical models, which can accurately quantify the amount of biological matter bound to the mologram from the diffracted intensity. In addition, it presents measurements of diffraction-limited molographic foci, i.e., Airy discs. These improvements enable us to demonstrate a resolution in real-time binding experiments comparable to the best SPR sensors without the need for temperature stabilization or drift correction and to detect low-molecular-weight compounds label free in an endpoint format. The presented experiments exemplify the robustness and sensitivity of the diffractometric sensor principle.},
note = {test},
keywords = {},
pubstate = {published},
tppubtype = {article}
}

@article{Frutiger2018,
title = {Image reversal reactive immersion lithography improves the detection limit of focal molography},
author = {Andreas Frutiger and Cla Duri Tschannen and Yves Blickenstorfer and Andreas M Reichmuth and Christof Fattinger and Janos Vörös},
doi = {10.1364/ol.43.005801},
issn = {0146-9592},
year = {2018},
date = {2018-01-01},
journal = {Optics Letters},
volume = {43},
number = {23},
pages = {5801},
abstract = {Focal molography is a label-free optical biosensing method that relies on a coherent pattern of binding sites for biomolecular interaction analysis. Reactive immersion lithography (RIL) is central to the patterning of molographic chips but has potential for improvements. Here, we show that applying the idea of image reversal to RIL enables the fabrication of coherent binding patterns of increased quality (i.e., higher analyte efficiency). Thereby the detection limit of focal molography in biological assays can be improved.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}