@article{51121,
  abstract     = {{<jats:p>DNA origami nanostructures are a powerful tool in biomedicine and can be used to combat drug‐resistant bacterial infections. However, the effect of unmodified DNA origami nanostructures on bacteria is yet to be elucidated. With the aim to obtain a better understanding of this phenomenon, the effect of three DNA origami shapes, i.e., DNA origami triangles, six‐helix bundles (6HBs), and 24‐helix bundles (24HBs), on the growth of Gram‐negative Escherichia coli and Gram‐positive Bacillus subtilis is investigated. These results reveal that while triangles and 24HBs can be used as a source of nutrients by E. coli and thereby promote population growth, their effect is much smaller than that of genomic single‐ and double‐stranded DNA. However, no effect on E. coli population growth is observed for the 6HBs. On the other hand, B. subtilis does not show any significant changes in population growth when cultured with the different DNA origami shapes or genomic DNA. The detailed effect of DNA origami nanostructures on bacterial growth thus depends on the competence signals and uptake mechanism of each bacterial species, as well as the DNA origami shape. This should be considered in the development of antimicrobial DNA origami nanostructures.</jats:p>}},
  author       = {{Garcia-Diosa, Jaime Andres and Grundmeier, Guido and Keller, Adrian}},
  issn         = {{1439-4227}},
  journal      = {{ChemBioChem}},
  keywords     = {{Organic Chemistry, Molecular Biology, Molecular Medicine, Biochemistry}},
  publisher    = {{Wiley}},
  title        = {{{Effect of DNA Origami Nanostructures on Bacterial Growth}}},
  doi          = {{10.1002/cbic.202400091}},
  year         = {{2024}},
}

@article{46023,
  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}},
  publisher    = {{MDPI AG}},
  title        = {{{Electrode Potential-Dependent Studies of Protein Adsorption on Ti6Al4V Alloy}}},
  doi          = {{10.3390/molecules28135109}},
  volume       = {{28}},
  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{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}},
}

@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{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{32323,
  abstract     = {{<jats:p>Genetic correlations suggest a coexisting genetic predisposition to both low leptin levels and risk for anorexia nervosa (AN). To investigate the causality and direction of these associations, we performed bidirectional two-sample Mendelian randomization (MR) analyses using data of the most recent genome-wide association study (GWAS) for AN and both a GWAS and an exome-wide-association-study (EWAS) for leptin levels. Most MR methods with genetic instruments from GWAS showed a causal effect of lower leptin levels on higher risk of AN (e.g. IVW b = −0.923, <jats:italic>p</jats:italic> = 1.5 × 10<jats:sup>−4</jats:sup>). Because most patients with AN are female, we additionally performed analyses using leptin GWAS data of females only. Again, there was a significant effect of leptin levels on the risk of AN (e.g. IVW b = −0.826, <jats:italic>p</jats:italic> = 1.1 × 10<jats:sup>−04</jats:sup>). MR with genetic instruments from EWAS showed no overall effect of leptin levels on the risk for AN. For the opposite direction, MR revealed no causal effect of AN on leptin levels. If our results are confirmed in extended GWAS data sets, a low endogenous leptin synthesis represents a risk factor for developing AN.</jats:p>}},
  author       = {{Peters, Triinu and Antel, Jochen and Naaresh, Roaa and Laabs, Björn-Hergen and Föcker, Manuel and Albers, Nicola and Bühlmeier, Judith and Hinney, Anke and Libuda, Lars and Hebebrand, Johannes}},
  issn         = {{1664-8021}},
  journal      = {{Frontiers in Genetics}},
  keywords     = {{Genetics (clinical), Genetics, Molecular Medicine}},
  publisher    = {{Frontiers Media SA}},
  title        = {{{Suggestive Evidence for Causal Effect of Leptin Levels on Risk for Anorexia Nervosa: Results of a Mendelian Randomization Study}}},
  doi          = {{10.3389/fgene.2021.733606}},
  volume       = {{12}},
  year         = {{2021}},
}