@article{48013,
  author       = {{Liu, Ping and Schumann, Nils and Abele, Fabian and Ren, Fazheng and Hanke, Marcel and Xin, Yang and Hartmann, Andreas and Schlierf, Michael and Keller, Adrian and Lin, Weilin and Zhang, Yixin}},
  issn         = {{2574-0970}},
  journal      = {{ACS Applied Nano Materials}},
  keywords     = {{General Materials Science}},
  publisher    = {{American Chemical Society (ACS)}},
  title        = {{{Thermophoretic Analysis of Biomolecules across the Nanoscales in Self-Assembled Polymeric Matrices}}},
  doi          = {{10.1021/acsanm.3c03623}},
  year         = {{2023}},
}

@article{48588,
  abstract     = {{<jats:p>Bacterial colonization and biofilm formation on abiotic surfaces are initiated by the adhesion of peptides and proteins. Understanding the adhesion of such peptides and proteins at a molecular level thus represents an important step toward controlling and suppressing biofilm formation on technological and medical materials. This study investigates the molecular adhesion of a pilus‐derived peptide that facilitates biofilm formation of Pseudomonas aeruginosa, a multidrug‐resistant opportunistic pathogen frequently encountered in healthcare settings. Single‐molecule force spectroscopy (SMFS) was performed on chemically etched ZnO surfaces to gather insights about peptide adsorption force and its kinetics. Metal‐free click chemistry for the fabrication of peptide‐terminated SMFS cantilevers was performed on amine‐terminated gold cantilevers and verified by X‐ray photoelectron spectroscopy (XPS) and polarization‐modulated infrared reflection absorption spectroscopy (PM‐IRRAS). Atomic force microscopy (AFM) and XPS analyses reveal stable topographies and surface chemistries of the substrates that are not affected by SMFS. Rupture events described by the worm‐like chain model (WLC) up to 600 pN were detected for the non‐polar ZnO(11‐20) surfaces. The dissociation barrier energy at zero force ΔG(0), the transition state distance xb and bound‐unbound dissociation rate at zero force koff(0) for the single crystalline substrate indicate that coordination and hydrogen bonds dominate the peptide/surface interaction.</jats:p>}},
  author       = {{Prüßner, Tim and Meinderink, Dennis and Zhu, Siqi and Orive, Alejandro G. and Kielar, Charlotte and Huck, Marten and Steinrück, Hans-Georg and Keller, Adrian and Grundmeier, Guido}},
  issn         = {{0947-6539}},
  journal      = {{Chemistry – A European Journal}},
  keywords     = {{General Chemistry, Catalysis, Organic Chemistry}},
  publisher    = {{Wiley}},
  title        = {{{Molecular Adhesion of a Pilus‐derived Peptide Involved in Pseudomonas aeruginosa Biofilm Formation on non‐polar ZnO Surfaces}}},
  doi          = {{10.1002/chem.202302464}},
  year         = {{2023}},
}

@article{33447,
  author       = {{Julin, Sofia and Keller, Adrian and Linko, Veikko}},
  issn         = {{1043-1802}},
  journal      = {{Bioconjugate Chemistry}},
  keywords     = {{Organic Chemistry, Pharmaceutical Science, Pharmacology, Biomedical Engineering, Bioengineering, Biotechnology}},
  pages        = {{18--29}},
  publisher    = {{American Chemical Society (ACS)}},
  title        = {{{Dynamics of DNA Origami Lattices}}},
  doi          = {{10.1021/acs.bioconjchem.2c00359}},
  volume       = {{34}},
  year         = {{2023}},
}

@article{42517,
  author       = {{Tapio, Kosti and Kielar, Charlotte and Parikka, Johannes M. and Keller, Adrian and Järvinen, Heini and Fahmy, Karim and Toppari, J. Jussi}},
  issn         = {{0897-4756}},
  journal      = {{Chemistry of Materials}},
  keywords     = {{Materials Chemistry, General Chemical Engineering, General Chemistry}},
  pages        = {{1961–1971}},
  publisher    = {{American Chemical Society (ACS)}},
  title        = {{{Large-Scale Formation of DNA Origami Lattices on Silicon}}},
  doi          = {{10.1021/acs.chemmater.2c03190}},
  volume       = {{35}},
  year         = {{2023}},
}

@article{42518,
  author       = {{Pothineni, Bhanu Kiran and Keller, Adrian}},
  issn         = {{2699-9307}},
  journal      = {{Advanced NanoBiomed Research}},
  keywords     = {{General Medicine}},
  publisher    = {{Wiley}},
  title        = {{{Nanoparticle‐Based Formulations of Glycopeptide Antibiotics: A Means for Overcoming Vancomycin Resistance in Bacterial Pathogens?}}},
  doi          = {{10.1002/anbr.202200134}},
  volume       = {{3}},
  year         = {{2023}},
}

@article{44503,
  author       = {{Hanke, Marcel and Tomm, Emilia and Grundmeier, Guido and Keller, Adrian}},
  issn         = {{1439-4227}},
  journal      = {{ChemBioChem}},
  keywords     = {{Organic Chemistry, Molecular Biology, Molecular Medicine, Biochemistry}},
  publisher    = {{Wiley}},
  title        = {{{Effect of Ionic Strength on the Thermal Stability of DNA Origami Nanostructures}}},
  doi          = {{10.1002/cbic.202300338}},
  year         = {{2023}},
}

@article{44504,
  author       = {{Linko, Veikko and Keller, Adrian}},
  issn         = {{1613-6810}},
  journal      = {{Small}},
  keywords     = {{Biomaterials, Biotechnology, General Materials Science, General Chemistry}},
  publisher    = {{Wiley}},
  title        = {{{Stability of DNA Origami Nanostructures in Physiological Media: The Role of Molecular Interactions}}},
  doi          = {{10.1002/smll.202301935}},
  year         = {{2023}},
}

@article{45828,
  abstract     = {{<jats:p>This article presents the potential-dependent adsorption of two proteins, bovine serum albumin (BSA) and lysozyme (LYZ), on Ti6Al4V alloy at pH 7.4 and 37 °C. The adsorption process was studied on an electropolished alloy under cathodic and anodic overpotentials, compared to the open circuit potential (OCP). To analyze the adsorption process, various complementary interface analytical techniques were employed, including PM-IRRAS (polarization-modulation infrared reflection-absorption spectroscopy), AFM (atomic force microscopy), XPS (X-ray photoelectron spectroscopy), and E-QCM (electrochemical quartz crystal microbalance) measurements. The polarization experiments were conducted within a potential range where charging of the electric double layer dominates, and Faradaic currents can be disregarded. The findings highlight the significant influence of the interfacial charge distribution on the adsorption of BSA and LYZ onto the alloy surface. Furthermore, electrochemical analysis of the protein layers formed under applied overpotentials demonstrated improved corrosion protection properties. These studies provide valuable insights into protein adsorption on titanium alloys under physiological conditions, characterized by varying potentials of the passive alloy.</jats:p>}},
  author       = {{Duderija, Belma and González-Orive, Alejandro and Ebbert, Christoph and Neßlinger, Vanessa and Keller, Adrian and Grundmeier, Guido}},
  issn         = {{1420-3049}},
  journal      = {{Molecules}},
  keywords     = {{Chemistry (miscellaneous), Analytical Chemistry, Organic Chemistry, Physical and Theoretical Chemistry, Molecular Medicine, Drug Discovery, Pharmaceutical Science}},
  number       = {{13}},
  pages        = {{5109}},
  publisher    = {{MDPI AG}},
  title        = {{{Electrode Potential-Dependent Studies of Protein Adsorption on Ti6Al4V Alloy}}},
  doi          = {{10.3390/molecules28135109}},
  volume       = {{28}},
  year         = {{2023}},
}

@inbook{45829,
  author       = {{Keller, Adrian and Grundmeier, Guido}},
  booktitle    = {{Reference Module in Chemistry, Molecular Sciences and Chemical Engineering}},
  isbn         = {{9780124095472}},
  publisher    = {{Elsevier}},
  title        = {{{High-speed AFM studies of macromolecular dynamics at solid/liquid interfaces}}},
  doi          = {{10.1016/b978-0-323-85669-0.00123-9}},
  year         = {{2023}},
}

@article{46061,
  abstract     = {{<jats:p>DNA origami nanostructures have emerged as functional materials for applications in various areas of science and technology. In particular, the transfer of the DNA origami shape into inorganic materials using...</jats:p>}},
  author       = {{Pothineni, Bhanu Kiran and Grundmeier, Guido and Keller, Adrian}},
  issn         = {{2040-3364}},
  journal      = {{Nanoscale}},
  keywords     = {{General Materials Science}},
  publisher    = {{Royal Society of Chemistry (RSC)}},
  title        = {{{Cation-dependent assembly of hexagonal DNA origami lattices on SiO2 surfaces}}},
  doi          = {{10.1039/d3nr02926c}},
  year         = {{2023}},
}

@article{46542,
  abstract     = {{<jats:p>Multiprotein adsorption from complex body fluids represents a highly important and complicated phenomenon in medicine. In this work, multiprotein adsorption from diluted human serum at gold and oxidized iron surfaces is investigated at different serum concentrations and pH values. Adsorption-induced changes in surface topography and the total amount of adsorbed proteins are quantified by atomic force microscopy (AFM) and polarization-modulation infrared reflection absorption spectroscopy (PM-IRRAS), respectively. For both surfaces, stronger protein adsorption is observed at pH 6 compared to pH 7 and pH 8. PM-IRRAS furthermore provides some qualitative insights into the pH-dependent alterations in the composition of the adsorbed multiprotein films. Changes in the amide II/amide I band area ratio and in particular side-chain IR absorption suggest that the increased adsorption at pH 6 is accompanied by a change in protein film composition. Presumably, this is mostly driven by the adsorption of human serum albumin, which at pH 6 adsorbs more readily and thereby replaces other proteins with lower surface affinities in the resulting multiprotein film.</jats:p>}},
  author       = {{Huang, Jingyuan and Qiu, Yunshu and Lücke, Felix and Su, Jiangling and Grundmeier, Guido and Keller, Adrian}},
  issn         = {{1420-3049}},
  journal      = {{Molecules}},
  keywords     = {{Chemistry (miscellaneous), Analytical Chemistry, Organic Chemistry, Physical and Theoretical Chemistry, Molecular Medicine, Drug Discovery, Pharmaceutical Science}},
  number       = {{16}},
  publisher    = {{MDPI AG}},
  title        = {{{Multiprotein Adsorption from Human Serum at Gold and Oxidized Iron Surfaces Studied by Atomic Force Microscopy and Polarization-Modulation Infrared Reflection Absorption Spectroscopy}}},
  doi          = {{10.3390/molecules28166060}},
  volume       = {{28}},
  year         = {{2023}},
}

@article{46543,
  abstract     = {{<jats:p>The influence of nanoscale surface topography on protein adsorption is highly important for numerous applications in medicine and technology. Herein, ferritin adsorption at flat and nanofaceted, single-crystalline Al2O3 surfaces is investigated using atomic force microscopy and X-ray photoelectron spectroscopy. The nanofaceted surfaces are generated by the thermal annealing of Al2O3 wafers at temperatures above 1000 °C, which leads to the formation of faceted saw-tooth-like surface topographies with periodicities of about 160 nm and amplitudes of about 15 nm. Ferritin adsorption at these nanofaceted surfaces is notably suppressed compared to the flat surface at a concentration of 10 mg/mL, which is attributed to lower adsorption affinities of the newly formed facets. Consequently, adsorption is restricted mostly to the pattern grooves, where the proteins can maximize their contact area with the surface. However, this effect depends on the protein concentration, with an inverse trend being observed at 30 mg/mL. Furthermore, different ferritin adsorption behavior is observed at topographically similar nanofacet patterns fabricated at different annealing temperatures and attributed to different step and kink densities. These results demonstrate that while protein adsorption at solid surfaces can be notably affected by nanofacet patterns, fine-tuning protein adsorption in this way requires the precise control of facet properties.</jats:p>}},
  author       = {{Pothineni, Bhanu K. and Kollmann, Sabrina and Li, Xinyang and Grundmeier, Guido and Erb, Denise J. and Keller, Adrian}},
  issn         = {{1422-0067}},
  journal      = {{International Journal of Molecular Sciences}},
  keywords     = {{Inorganic Chemistry, Organic Chemistry, Physical and Theoretical Chemistry, Computer Science Applications, Spectroscopy, Molecular Biology, General Medicine, Catalysis}},
  number       = {{16}},
  publisher    = {{MDPI AG}},
  title        = {{{Adsorption of Ferritin at Nanofaceted Al2O3 Surfaces}}},
  doi          = {{10.3390/ijms241612808}},
  volume       = {{24}},
  year         = {{2023}},
}

@article{47140,
  abstract     = {{<jats:p>The structural stability of DNA origami nanostructures in various chemical environments is an important factor in numerous applications, ranging from biomedicine and biophysics to analytical chemistry and materials synthesis. In...</jats:p>}},
  author       = {{Hanke, Marcel and Dornbusch, Daniel and Tomm, Emilia and Grundmeier, Guido and Fahmy, Karim and Keller, Adrian}},
  issn         = {{2040-3364}},
  journal      = {{Nanoscale}},
  keywords     = {{General Materials Science}},
  publisher    = {{Royal Society of Chemistry (RSC)}},
  title        = {{{Superstructure-dependent stability of DNA origami nanostructures in the presence of chaotropic denaturants}}},
  doi          = {{10.1039/d3nr02045b}},
  year         = {{2023}},
}

@article{30738,
  author       = {{Xin, Yang and Piskunen, Petteri and Suma, Antonio and Li, Changyong and Ijäs, Heini and Ojasalo, Sofia and Seitz, Iris and Kostiainen, Mauri A. and Grundmeier, Guido and Linko, Veikko and Keller, Adrian}},
  issn         = {{1613-6810}},
  journal      = {{Small}},
  keywords     = {{Biomaterials, Biotechnology, General Materials Science, General Chemistry}},
  pages        = {{2107393}},
  publisher    = {{Wiley}},
  title        = {{{Environment‐Dependent Stability and Mechanical Properties of DNA Origami Six‐Helix Bundles with Different Crossover Spacings}}},
  doi          = {{10.1002/smll.202107393}},
  volume       = {{18}},
  year         = {{2022}},
}

@article{29806,
  author       = {{Huang, Jingyuan and Voigt, Markus and Wackenrohr, Steffen and Ebbert, Christoph and Keller, Adrian and Maier, Hans Jürgen and Grundmeier, Guido}},
  issn         = {{0947-5117}},
  journal      = {{Materials and Corrosion}},
  keywords     = {{Materials Chemistry, Metals and Alloys, Surfaces, Coatings and Films, Mechanical Engineering, Mechanics of Materials, Environmental Chemistry, Materials Chemistry, Metals and Alloys, Surfaces, Coatings and Films, Mechanical Engineering, Mechanics of Materials, Environmental Chemistry, Materials Chemistry, Metals and Alloys, Surfaces, Coatings and Films, Mechanical Engineering, Mechanics of Materials, Environmental Chemistry}},
  pages        = {{1034}},
  publisher    = {{Wiley}},
  title        = {{{Influence of hydrogel coatings on corrosion and fatigue of iron in simulated body fluid}}},
  doi          = {{10.1002/maco.202112841}},
  volume       = {{73}},
  year         = {{2022}},
}

@article{32432,
  author       = {{Yang, Yu and Huang, Jingyuan and Dornbusch, Daniel and Grundmeier, Guido and Fahmy, Karim and Keller, Adrian and Cheung, David L.}},
  issn         = {{0743-7463}},
  journal      = {{Langmuir}},
  keywords     = {{Electrochemistry, Spectroscopy, Surfaces and Interfaces, Condensed Matter Physics, General Materials Science}},
  pages        = {{9257–9265}},
  publisher    = {{American Chemical Society (ACS)}},
  title        = {{{Effect of Surface Hydrophobicity on the Adsorption of a Pilus-Derived Adhesin-like Peptide}}},
  doi          = {{10.1021/acs.langmuir.2c01016}},
  volume       = {{38}},
  year         = {{2022}},
}

@article{32589,
  abstract     = {{<jats:p>Guanidinium (Gdm) undergoes interactions with both hydrophilic and hydrophobic groups and, thus, is a highly potent denaturant of biomolecular structure. However, our molecular understanding of the interaction of Gdm with proteins and DNA is still rather limited. Here, we investigated the denaturation of DNA origami nanostructures by three Gdm salts, i.e., guanidinium chloride (GdmCl), guanidinium sulfate (Gdm2SO4), and guanidinium thiocyanate (GdmSCN), at different temperatures and in dependence of incubation time. Using DNA origami nanostructures as sensors that translate small molecular transitions into nanostructural changes, the denaturing effects of the Gdm salts were directly visualized by atomic force microscopy. GdmSCN was the most potent DNA denaturant, which caused complete DNA origami denaturation at 50 °C already at a concentration of 2 M. Under such harsh conditions, denaturation occurred within the first 15 min of Gdm exposure, whereas much slower kinetics were observed for the more weakly denaturing salt Gdm2SO4 at 25 °C. Lastly, we observed a novel non-monotonous temperature dependence of DNA origami denaturation in Gdm2SO4 with the fraction of intact nanostructures having an intermediate minimum at about 40 °C. Our results, thus, provide further insights into the highly complex Gdm–DNA interaction and underscore the importance of the counteranion species.</jats:p>}},
  author       = {{Hanke, Marcel and Hansen, Niklas and Tomm, Emilia and Grundmeier, Guido and Keller, Adrian}},
  issn         = {{1422-0067}},
  journal      = {{International Journal of Molecular Sciences}},
  keywords     = {{Inorganic Chemistry, Organic Chemistry, Physical and Theoretical Chemistry, Computer Science Applications, Spectroscopy, Molecular Biology, General Medicine, Catalysis}},
  number       = {{15}},
  pages        = {{8547}},
  publisher    = {{MDPI AG}},
  title        = {{{Time-Dependent DNA Origami Denaturation by Guanidinium Chloride, Guanidinium Sulfate, and Guanidinium Thiocyanate}}},
  doi          = {{10.3390/ijms23158547}},
  volume       = {{23}},
  year         = {{2022}},
}

@article{33446,
  author       = {{Dreher, Yannik and Fichtler, Julius and Karfusehr, Christoph and Jahnke, Kevin and Xin, Yang and Keller, Adrian and Göpfrich, Kerstin}},
  issn         = {{0006-3495}},
  journal      = {{Biophysical Journal}},
  keywords     = {{Biophysics}},
  pages        = {{4840--4848}},
  publisher    = {{Elsevier BV}},
  title        = {{{Genotype-phenotype mapping with polyominos made from DNA origami tiles}}},
  doi          = {{10.1016/j.bpj.2022.09.006}},
  volume       = {{121}},
  year         = {{2022}},
}

@article{30739,
  author       = {{Ring, Julia and Tadic, Jelena and Ristic, Selena and Poglitsch, Michael and Bergmann, Martina and Radic, Nemanja and Mossmann, Dirk and Liang, YongTian and Maglione, Marta and Jerkovic, Andrea and Hajiraissi, Roozbeh and Hanke, Marcel and Küttner, Victoria and Wolinski, Heimo and Zimmermann, Andreas and Domuz Trifunović, Lana and Mikolasch, Leonie and Moretti, Daiana N and Broeskamp, Filomena and Westermayer, Julia and Abraham, Claudia and Schauer, Simon and Dammbrueck, Christopher and Hofer, Sebastian J and Abdellatif, Mahmoud and Grundmeier, Guido and Kroemer, Guido and Braun, Ralf J and Hansen, Niklas and Sommer, Cornelia and Ninkovic, Mirjana and Seba, Sandra and Rockenfeller, Patrick and Vögtle, Friederike‐Nora and Dengjel, Jörn and Meisinger, Chris and Keller, Adrian and Sigrist, Stephan J and Eisenberg, Tobias and Madeo, Frank}},
  issn         = {{1757-4676}},
  journal      = {{EMBO Molecular Medicine}},
  keywords     = {{Molecular Medicine}},
  pages        = {{e13952}},
  publisher    = {{EMBO}},
  title        = {{{The HSP40 chaperone Ydj1 drives amyloid beta 42 toxicity}}},
  doi          = {{10.15252/emmm.202113952}},
  volume       = {{14}},
  year         = {{2022}},
}

@article{31547,
  author       = {{Hanke, Marcel and Dornbusch, Daniel and Hadlich, Christoph and Rossberg, Andre and Hansen, Niklas and Grundmeier, Guido and Tsushima, Satoru and Keller, Adrian and Fahmy, Karim}},
  issn         = {{2001-0370}},
  journal      = {{Computational and Structural Biotechnology Journal}},
  keywords     = {{Computer Science Applications, Genetics, Biochemistry, Structural Biology, Biophysics, Biotechnology}},
  pages        = {{2611--2623}},
  publisher    = {{Elsevier BV}},
  title        = {{{Anion-specific structure and stability of guanidinium-bound DNA origami}}},
  doi          = {{10.1016/j.csbj.2022.05.037}},
  volume       = {{20}},
  year         = {{2022}},
}