[{"language":[{"iso":"eng"}],"keyword":["Inorganic Chemistry","Organic Chemistry","Physical and Theoretical Chemistry","Computer Science Applications","Spectroscopy","Molecular Biology","General Medicine","Catalysis"],"article_number":"7226","user_id":"67287","_id":"50150","project":[{"_id":"52","name":"PC2: Computing Resources Provided by the Paderborn Center for Parallel Computing"}],"status":"public","abstract":[{"lang":"eng","text":"<jats:p>Covalent peptidomimetic protease inhibitors have gained a lot of attention in drug development in recent years. They are designed to covalently bind the catalytically active amino acids through electrophilic groups called warheads. Covalent inhibition has an advantage in terms of pharmacodynamic properties but can also bear toxicity risks due to non-selective off-target protein binding. Therefore, the right combination of a reactive warhead with a well-suited peptidomimetic sequence is of great importance. Herein, the selectivities of well-known warheads combined with peptidomimetic sequences suited for five different proteases were investigated, highlighting the impact of both structure parts (warhead and peptidomimetic sequence) for affinity and selectivity. Molecular docking gave insights into the predicted binding modes of the inhibitors inside the binding pockets of the different enzymes. Moreover, the warheads were investigated by NMR and LC-MS reactivity assays against serine/threonine and cysteine nucleophile models, as well as by quantum mechanics simulations.</jats:p>"}],"publication":"International Journal of Molecular Sciences","type":"journal_article","doi":"10.3390/ijms24087226","title":"Investigation of the Compatibility between Warheads and Peptidomimetic Sequences of Protease Inhibitors—A Comprehensive Reactivity and Selectivity Study","volume":24,"author":[{"first_name":"Patrick","last_name":"Müller","full_name":"Müller, Patrick"},{"last_name":"Meta","full_name":"Meta, Mergim","first_name":"Mergim"},{"first_name":"Jan Laurenz","last_name":"Meidner","full_name":"Meidner, Jan Laurenz"},{"full_name":"Schwickert, Marvin","last_name":"Schwickert","first_name":"Marvin"},{"first_name":"Jessica","last_name":"Meyr","full_name":"Meyr, Jessica"},{"first_name":"Kevin","full_name":"Schwickert, Kevin","last_name":"Schwickert"},{"first_name":"Christian","full_name":"Kersten, Christian","last_name":"Kersten"},{"last_name":"Zimmer","full_name":"Zimmer, Collin","first_name":"Collin"},{"first_name":"Stefan Josef","last_name":"Hammerschmidt","full_name":"Hammerschmidt, Stefan Josef"},{"first_name":"Ariane","last_name":"Frey","full_name":"Frey, Ariane"},{"first_name":"Albin","last_name":"Lahu","full_name":"Lahu, Albin"},{"first_name":"Sergio","full_name":"de la Hoz-Rodríguez, Sergio","last_name":"de la Hoz-Rodríguez"},{"full_name":"Agost-Beltrán, Laura","last_name":"Agost-Beltrán","first_name":"Laura"},{"first_name":"Santiago","last_name":"Rodríguez","full_name":"Rodríguez, Santiago"},{"first_name":"Kira","full_name":"Diemer, Kira","last_name":"Diemer"},{"full_name":"Neumann, Wilhelm","last_name":"Neumann","first_name":"Wilhelm"},{"first_name":"Florenci V.","last_name":"Gonzàlez","full_name":"Gonzàlez, Florenci V."},{"full_name":"Engels, Bernd","last_name":"Engels","first_name":"Bernd"},{"first_name":"Tanja","full_name":"Schirmeister, Tanja","last_name":"Schirmeister"}],"date_created":"2024-01-04T08:24:31Z","date_updated":"2024-01-05T12:59:32Z","publisher":"MDPI AG","intvolume":"        24","citation":{"bibtex":"@article{Müller_Meta_Meidner_Schwickert_Meyr_Schwickert_Kersten_Zimmer_Hammerschmidt_Frey_et al._2023, title={Investigation of the Compatibility between Warheads and Peptidomimetic Sequences of Protease Inhibitors—A Comprehensive Reactivity and Selectivity Study}, volume={24}, DOI={<a href=\"https://doi.org/10.3390/ijms24087226\">10.3390/ijms24087226</a>}, number={87226}, journal={International Journal of Molecular Sciences}, publisher={MDPI AG}, author={Müller, Patrick and Meta, Mergim and Meidner, Jan Laurenz and Schwickert, Marvin and Meyr, Jessica and Schwickert, Kevin and Kersten, Christian and Zimmer, Collin and Hammerschmidt, Stefan Josef and Frey, Ariane and et al.}, year={2023} }","mla":"Müller, Patrick, et al. “Investigation of the Compatibility between Warheads and Peptidomimetic Sequences of Protease Inhibitors—A Comprehensive Reactivity and Selectivity Study.” <i>International Journal of Molecular Sciences</i>, vol. 24, no. 8, 7226, MDPI AG, 2023, doi:<a href=\"https://doi.org/10.3390/ijms24087226\">10.3390/ijms24087226</a>.","short":"P. Müller, M. Meta, J.L. Meidner, M. Schwickert, J. Meyr, K. Schwickert, C. Kersten, C. Zimmer, S.J. Hammerschmidt, A. Frey, A. Lahu, S. de la Hoz-Rodríguez, L. Agost-Beltrán, S. Rodríguez, K. Diemer, W. Neumann, F.V. Gonzàlez, B. Engels, T. Schirmeister, International Journal of Molecular Sciences 24 (2023).","apa":"Müller, P., Meta, M., Meidner, J. L., Schwickert, M., Meyr, J., Schwickert, K., Kersten, C., Zimmer, C., Hammerschmidt, S. J., Frey, A., Lahu, A., de la Hoz-Rodríguez, S., Agost-Beltrán, L., Rodríguez, S., Diemer, K., Neumann, W., Gonzàlez, F. V., Engels, B., &#38; Schirmeister, T. (2023). Investigation of the Compatibility between Warheads and Peptidomimetic Sequences of Protease Inhibitors—A Comprehensive Reactivity and Selectivity Study. <i>International Journal of Molecular Sciences</i>, <i>24</i>(8), Article 7226. <a href=\"https://doi.org/10.3390/ijms24087226\">https://doi.org/10.3390/ijms24087226</a>","ieee":"P. Müller <i>et al.</i>, “Investigation of the Compatibility between Warheads and Peptidomimetic Sequences of Protease Inhibitors—A Comprehensive Reactivity and Selectivity Study,” <i>International Journal of Molecular Sciences</i>, vol. 24, no. 8, Art. no. 7226, 2023, doi: <a href=\"https://doi.org/10.3390/ijms24087226\">10.3390/ijms24087226</a>.","chicago":"Müller, Patrick, Mergim Meta, Jan Laurenz Meidner, Marvin Schwickert, Jessica Meyr, Kevin Schwickert, Christian Kersten, et al. “Investigation of the Compatibility between Warheads and Peptidomimetic Sequences of Protease Inhibitors—A Comprehensive Reactivity and Selectivity Study.” <i>International Journal of Molecular Sciences</i> 24, no. 8 (2023). <a href=\"https://doi.org/10.3390/ijms24087226\">https://doi.org/10.3390/ijms24087226</a>.","ama":"Müller P, Meta M, Meidner JL, et al. Investigation of the Compatibility between Warheads and Peptidomimetic Sequences of Protease Inhibitors—A Comprehensive Reactivity and Selectivity Study. <i>International Journal of Molecular Sciences</i>. 2023;24(8). doi:<a href=\"https://doi.org/10.3390/ijms24087226\">10.3390/ijms24087226</a>"},"year":"2023","issue":"8","publication_identifier":{"issn":["1422-0067"]},"publication_status":"published"},{"citation":{"chicago":"Pothineni, Bhanu K., Sabrina Kollmann, Xinyang Li, Guido Grundmeier, Denise J. Erb, and Adrian Keller. “Adsorption of Ferritin at Nanofaceted Al2O3 Surfaces.” <i>International Journal of Molecular Sciences</i> 24, no. 16 (2023). <a href=\"https://doi.org/10.3390/ijms241612808\">https://doi.org/10.3390/ijms241612808</a>.","ieee":"B. K. Pothineni, S. Kollmann, X. Li, G. Grundmeier, D. J. Erb, and A. Keller, “Adsorption of Ferritin at Nanofaceted Al2O3 Surfaces,” <i>International Journal of Molecular Sciences</i>, vol. 24, no. 16, Art. no. 12808, 2023, doi: <a href=\"https://doi.org/10.3390/ijms241612808\">10.3390/ijms241612808</a>.","ama":"Pothineni BK, Kollmann S, Li X, Grundmeier G, Erb DJ, Keller A. Adsorption of Ferritin at Nanofaceted Al2O3 Surfaces. <i>International Journal of Molecular Sciences</i>. 2023;24(16). doi:<a href=\"https://doi.org/10.3390/ijms241612808\">10.3390/ijms241612808</a>","apa":"Pothineni, B. K., Kollmann, S., Li, X., Grundmeier, G., Erb, D. J., &#38; Keller, A. (2023). Adsorption of Ferritin at Nanofaceted Al2O3 Surfaces. <i>International Journal of Molecular Sciences</i>, <i>24</i>(16), Article 12808. <a href=\"https://doi.org/10.3390/ijms241612808\">https://doi.org/10.3390/ijms241612808</a>","short":"B.K. Pothineni, S. Kollmann, X. Li, G. Grundmeier, D.J. Erb, A. Keller, International Journal of Molecular Sciences 24 (2023).","bibtex":"@article{Pothineni_Kollmann_Li_Grundmeier_Erb_Keller_2023, title={Adsorption of Ferritin at Nanofaceted Al2O3 Surfaces}, volume={24}, DOI={<a href=\"https://doi.org/10.3390/ijms241612808\">10.3390/ijms241612808</a>}, number={1612808}, journal={International Journal of Molecular Sciences}, publisher={MDPI AG}, author={Pothineni, Bhanu K. and Kollmann, Sabrina and Li, Xinyang and Grundmeier, Guido and Erb, Denise J. and Keller, Adrian}, year={2023} }","mla":"Pothineni, Bhanu K., et al. “Adsorption of Ferritin at Nanofaceted Al2O3 Surfaces.” <i>International Journal of Molecular Sciences</i>, vol. 24, no. 16, 12808, MDPI AG, 2023, doi:<a href=\"https://doi.org/10.3390/ijms241612808\">10.3390/ijms241612808</a>."},"intvolume":"        24","year":"2023","issue":"16","publication_status":"published","publication_identifier":{"issn":["1422-0067"]},"doi":"10.3390/ijms241612808","title":"Adsorption of Ferritin at Nanofaceted Al2O3 Surfaces","date_created":"2023-08-16T10:52:25Z","author":[{"first_name":"Bhanu K.","full_name":"Pothineni, Bhanu K.","last_name":"Pothineni"},{"first_name":"Sabrina","full_name":"Kollmann, Sabrina","last_name":"Kollmann"},{"first_name":"Xinyang","last_name":"Li","full_name":"Li, Xinyang"},{"first_name":"Guido","last_name":"Grundmeier","id":"194","full_name":"Grundmeier, Guido"},{"last_name":"Erb","full_name":"Erb, Denise J.","first_name":"Denise J."},{"first_name":"Adrian","orcid":"0000-0001-7139-3110","last_name":"Keller","id":"48864","full_name":"Keller, Adrian"}],"volume":24,"publisher":"MDPI AG","date_updated":"2023-08-16T10:53:00Z","status":"public","abstract":[{"text":"<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>","lang":"eng"}],"type":"journal_article","publication":"International Journal of Molecular Sciences","language":[{"iso":"eng"}],"article_number":"12808","keyword":["Inorganic Chemistry","Organic Chemistry","Physical and Theoretical Chemistry","Computer Science Applications","Spectroscopy","Molecular Biology","General Medicine","Catalysis"],"user_id":"48864","department":[{"_id":"302"}],"_id":"46543"},{"publisher":"MDPI AG","date_created":"2022-03-07T07:28:02Z","title":"Salting-Out of DNA Origami Nanostructures by Ammonium Sulfate","issue":"5","year":"2022","keyword":["Inorganic Chemistry","Organic Chemistry","Physical and Theoretical Chemistry","Computer Science Applications","Spectroscopy","Molecular Biology","General Medicine","Catalysis"],"language":[{"iso":"eng"}],"publication":"International Journal of Molecular Sciences","abstract":[{"text":"<jats:p>DNA origami technology enables the folding of DNA strands into complex nanoscale shapes whose properties and interactions with molecular species often deviate significantly from that of genomic DNA. Here, we investigate the salting-out of different DNA origami shapes by the kosmotropic salt ammonium sulfate that is routinely employed in protein precipitation. We find that centrifugation in the presence of 3 M ammonium sulfate results in notable precipitation of DNA origami nanostructures but not of double-stranded genomic DNA. The precipitated DNA origami nanostructures can be resuspended in ammonium sulfate-free buffer without apparent formation of aggregates or loss of structural integrity. Even though quasi-1D six-helix bundle DNA origami are slightly less susceptible toward salting-out than more compact DNA origami triangles and 24-helix bundles, precipitation and recovery yields appear to be mostly independent of DNA origami shape and superstructure. Exploiting the specificity of ammonium sulfate salting-out for DNA origami nanostructures, we further apply this method to separate DNA origami triangles from genomic DNA fragments in a complex mixture. Our results thus demonstrate the possibility of concentrating and purifying DNA origami nanostructures by ammonium sulfate-induced salting-out.</jats:p>","lang":"eng"}],"date_updated":"2022-03-07T07:29:27Z","volume":23,"author":[{"first_name":"Marcel","last_name":"Hanke","full_name":"Hanke, Marcel"},{"last_name":"Hansen","full_name":"Hansen, Niklas","first_name":"Niklas"},{"last_name":"Chen","full_name":"Chen, Ruiping","first_name":"Ruiping"},{"first_name":"Guido","last_name":"Grundmeier","full_name":"Grundmeier, Guido"},{"last_name":"Fahmy","full_name":"Fahmy, Karim","first_name":"Karim"},{"full_name":"Keller, Adrian","last_name":"Keller","first_name":"Adrian"}],"doi":"10.3390/ijms23052817","publication_identifier":{"issn":["1422-0067"]},"publication_status":"published","page":"2817","intvolume":"        23","citation":{"chicago":"Hanke, Marcel, Niklas Hansen, Ruiping Chen, Guido Grundmeier, Karim Fahmy, and Adrian Keller. “Salting-Out of DNA Origami Nanostructures by Ammonium Sulfate.” <i>International Journal of Molecular Sciences</i> 23, no. 5 (2022): 2817. <a href=\"https://doi.org/10.3390/ijms23052817\">https://doi.org/10.3390/ijms23052817</a>.","ieee":"M. Hanke, N. Hansen, R. Chen, G. Grundmeier, K. Fahmy, and A. Keller, “Salting-Out of DNA Origami Nanostructures by Ammonium Sulfate,” <i>International Journal of Molecular Sciences</i>, vol. 23, no. 5, p. 2817, 2022, doi: <a href=\"https://doi.org/10.3390/ijms23052817\">10.3390/ijms23052817</a>.","ama":"Hanke M, Hansen N, Chen R, Grundmeier G, Fahmy K, Keller A. Salting-Out of DNA Origami Nanostructures by Ammonium Sulfate. <i>International Journal of Molecular Sciences</i>. 2022;23(5):2817. doi:<a href=\"https://doi.org/10.3390/ijms23052817\">10.3390/ijms23052817</a>","apa":"Hanke, M., Hansen, N., Chen, R., Grundmeier, G., Fahmy, K., &#38; Keller, A. (2022). Salting-Out of DNA Origami Nanostructures by Ammonium Sulfate. <i>International Journal of Molecular Sciences</i>, <i>23</i>(5), 2817. <a href=\"https://doi.org/10.3390/ijms23052817\">https://doi.org/10.3390/ijms23052817</a>","short":"M. Hanke, N. Hansen, R. Chen, G. Grundmeier, K. Fahmy, A. Keller, International Journal of Molecular Sciences 23 (2022) 2817.","mla":"Hanke, Marcel, et al. “Salting-Out of DNA Origami Nanostructures by Ammonium Sulfate.” <i>International Journal of Molecular Sciences</i>, vol. 23, no. 5, MDPI AG, 2022, p. 2817, doi:<a href=\"https://doi.org/10.3390/ijms23052817\">10.3390/ijms23052817</a>.","bibtex":"@article{Hanke_Hansen_Chen_Grundmeier_Fahmy_Keller_2022, title={Salting-Out of DNA Origami Nanostructures by Ammonium Sulfate}, volume={23}, DOI={<a href=\"https://doi.org/10.3390/ijms23052817\">10.3390/ijms23052817</a>}, number={5}, journal={International Journal of Molecular Sciences}, publisher={MDPI AG}, author={Hanke, Marcel and Hansen, Niklas and Chen, Ruiping and Grundmeier, Guido and Fahmy, Karim and Keller, Adrian}, year={2022}, pages={2817} }"},"_id":"30209","department":[{"_id":"302"}],"user_id":"48864","type":"journal_article","status":"public"},{"department":[{"_id":"302"}],"user_id":"48864","_id":"32589","language":[{"iso":"eng"}],"keyword":["Inorganic Chemistry","Organic Chemistry","Physical and Theoretical Chemistry","Computer Science Applications","Spectroscopy","Molecular Biology","General Medicine","Catalysis"],"publication":"International Journal of Molecular Sciences","type":"journal_article","status":"public","abstract":[{"text":"<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>","lang":"eng"}],"volume":23,"date_created":"2022-08-08T06:39:20Z","author":[{"first_name":"Marcel","full_name":"Hanke, Marcel","last_name":"Hanke"},{"last_name":"Hansen","full_name":"Hansen, Niklas","first_name":"Niklas"},{"first_name":"Emilia","last_name":"Tomm","full_name":"Tomm, Emilia"},{"first_name":"Guido","last_name":"Grundmeier","full_name":"Grundmeier, Guido","id":"194"},{"orcid":"0000-0001-7139-3110","last_name":"Keller","full_name":"Keller, Adrian","id":"48864","first_name":"Adrian"}],"publisher":"MDPI AG","date_updated":"2022-08-08T06:40:14Z","doi":"10.3390/ijms23158547","title":"Time-Dependent DNA Origami Denaturation by Guanidinium Chloride, Guanidinium Sulfate, and Guanidinium Thiocyanate","issue":"15","publication_identifier":{"issn":["1422-0067"]},"publication_status":"published","page":"8547","intvolume":"        23","citation":{"ama":"Hanke M, Hansen N, Tomm E, Grundmeier G, Keller A. Time-Dependent DNA Origami Denaturation by Guanidinium Chloride, Guanidinium Sulfate, and Guanidinium Thiocyanate. <i>International Journal of Molecular Sciences</i>. 2022;23(15):8547. doi:<a href=\"https://doi.org/10.3390/ijms23158547\">10.3390/ijms23158547</a>","chicago":"Hanke, Marcel, Niklas Hansen, Emilia Tomm, Guido Grundmeier, and Adrian Keller. “Time-Dependent DNA Origami Denaturation by Guanidinium Chloride, Guanidinium Sulfate, and Guanidinium Thiocyanate.” <i>International Journal of Molecular Sciences</i> 23, no. 15 (2022): 8547. <a href=\"https://doi.org/10.3390/ijms23158547\">https://doi.org/10.3390/ijms23158547</a>.","ieee":"M. Hanke, N. Hansen, E. Tomm, G. Grundmeier, and A. Keller, “Time-Dependent DNA Origami Denaturation by Guanidinium Chloride, Guanidinium Sulfate, and Guanidinium Thiocyanate,” <i>International Journal of Molecular Sciences</i>, vol. 23, no. 15, p. 8547, 2022, doi: <a href=\"https://doi.org/10.3390/ijms23158547\">10.3390/ijms23158547</a>.","mla":"Hanke, Marcel, et al. “Time-Dependent DNA Origami Denaturation by Guanidinium Chloride, Guanidinium Sulfate, and Guanidinium Thiocyanate.” <i>International Journal of Molecular Sciences</i>, vol. 23, no. 15, MDPI AG, 2022, p. 8547, doi:<a href=\"https://doi.org/10.3390/ijms23158547\">10.3390/ijms23158547</a>.","bibtex":"@article{Hanke_Hansen_Tomm_Grundmeier_Keller_2022, title={Time-Dependent DNA Origami Denaturation by Guanidinium Chloride, Guanidinium Sulfate, and Guanidinium Thiocyanate}, volume={23}, DOI={<a href=\"https://doi.org/10.3390/ijms23158547\">10.3390/ijms23158547</a>}, number={15}, journal={International Journal of Molecular Sciences}, publisher={MDPI AG}, author={Hanke, Marcel and Hansen, Niklas and Tomm, Emilia and Grundmeier, Guido and Keller, Adrian}, year={2022}, pages={8547} }","short":"M. Hanke, N. Hansen, E. Tomm, G. Grundmeier, A. Keller, International Journal of Molecular Sciences 23 (2022) 8547.","apa":"Hanke, M., Hansen, N., Tomm, E., Grundmeier, G., &#38; Keller, A. (2022). Time-Dependent DNA Origami Denaturation by Guanidinium Chloride, Guanidinium Sulfate, and Guanidinium Thiocyanate. <i>International Journal of Molecular Sciences</i>, <i>23</i>(15), 8547. <a href=\"https://doi.org/10.3390/ijms23158547\">https://doi.org/10.3390/ijms23158547</a>"},"year":"2022"},{"publication":"International Journal of Molecular Sciences","type":"journal_article","status":"public","abstract":[{"lang":"eng","text":"<jats:p>The effects that solid–liquid interfaces exert on the aggregation of proteins and peptides are of high relevance for various fields of basic and applied research, ranging from molecular biology and biomedicine to nanotechnology. While the influence of surface chemistry has received a lot of attention in this context, the role of surface topography has mostly been neglected so far. In this work, therefore, we investigate the aggregation of the type 2 diabetes-associated peptide hormone hIAPP in contact with flat and nanopatterned silicon oxide surfaces. The nanopatterned surfaces are produced by ion beam irradiation, resulting in well-defined anisotropic ripple patterns with heights and periodicities of about 1.5 and 30 nm, respectively. Using time-lapse atomic force microscopy, the morphology of the hIAPP aggregates is characterized quantitatively. Aggregation results in both amorphous aggregates and amyloid fibrils, with the presence of the nanopatterns leading to retarded fibrillization and stronger amorphous aggregation. This is attributed to structural differences in the amorphous aggregates formed at the nanopatterned surface, which result in a lower propensity for nucleating amyloid fibrillization. Our results demonstrate that nanoscale surface topography may modulate peptide and protein aggregation pathways in complex and intricate ways.</jats:p>"}],"department":[{"_id":"302"}],"user_id":"48864","_id":"22636","language":[{"iso":"eng"}],"publication_identifier":{"issn":["1422-0067"]},"publication_status":"published","page":"5142","intvolume":"        22","citation":{"bibtex":"@article{Hanke_Yang_Ji_Grundmeier_Keller_2021, title={Nanoscale Surface Topography Modulates hIAPP Aggregation Pathways at Solid–Liquid Interfaces}, volume={22}, DOI={<a href=\"https://doi.org/10.3390/ijms22105142\">10.3390/ijms22105142</a>}, journal={International Journal of Molecular Sciences}, author={Hanke, Marcel and Yang, Yu and Ji, Yuxin and Grundmeier, Guido and Keller, Adrian}, year={2021}, pages={5142} }","short":"M. Hanke, Y. Yang, Y. Ji, G. Grundmeier, A. Keller, International Journal of Molecular Sciences 22 (2021) 5142.","mla":"Hanke, Marcel, et al. “Nanoscale Surface Topography Modulates HIAPP Aggregation Pathways at Solid–Liquid Interfaces.” <i>International Journal of Molecular Sciences</i>, vol. 22, 2021, p. 5142, doi:<a href=\"https://doi.org/10.3390/ijms22105142\">10.3390/ijms22105142</a>.","apa":"Hanke, M., Yang, Y., Ji, Y., Grundmeier, G., &#38; Keller, A. (2021). Nanoscale Surface Topography Modulates hIAPP Aggregation Pathways at Solid–Liquid Interfaces. <i>International Journal of Molecular Sciences</i>, <i>22</i>, 5142. <a href=\"https://doi.org/10.3390/ijms22105142\">https://doi.org/10.3390/ijms22105142</a>","chicago":"Hanke, Marcel, Yu Yang, Yuxin Ji, Guido Grundmeier, and Adrian Keller. “Nanoscale Surface Topography Modulates HIAPP Aggregation Pathways at Solid–Liquid Interfaces.” <i>International Journal of Molecular Sciences</i> 22 (2021): 5142. <a href=\"https://doi.org/10.3390/ijms22105142\">https://doi.org/10.3390/ijms22105142</a>.","ieee":"M. Hanke, Y. Yang, Y. Ji, G. Grundmeier, and A. Keller, “Nanoscale Surface Topography Modulates hIAPP Aggregation Pathways at Solid–Liquid Interfaces,” <i>International Journal of Molecular Sciences</i>, vol. 22, p. 5142, 2021.","ama":"Hanke M, Yang Y, Ji Y, Grundmeier G, Keller A. Nanoscale Surface Topography Modulates hIAPP Aggregation Pathways at Solid–Liquid Interfaces. <i>International Journal of Molecular Sciences</i>. 2021;22:5142. doi:<a href=\"https://doi.org/10.3390/ijms22105142\">10.3390/ijms22105142</a>"},"year":"2021","volume":22,"date_created":"2021-07-08T11:43:14Z","author":[{"first_name":"Marcel","full_name":"Hanke, Marcel","last_name":"Hanke"},{"last_name":"Yang","full_name":"Yang, Yu","first_name":"Yu"},{"first_name":"Yuxin","last_name":"Ji","full_name":"Ji, Yuxin"},{"first_name":"Guido","id":"194","full_name":"Grundmeier, Guido","last_name":"Grundmeier"},{"first_name":"Adrian","last_name":"Keller","orcid":"0000-0001-7139-3110","full_name":"Keller, Adrian","id":"48864"}],"date_updated":"2022-01-06T06:55:37Z","doi":"10.3390/ijms22105142","title":"Nanoscale Surface Topography Modulates hIAPP Aggregation Pathways at Solid–Liquid Interfaces"},{"oa":"1","date_updated":"2025-12-03T16:52:35Z","volume":22,"author":[{"last_name":"Liu","full_name":"Liu, Zhibin","first_name":"Zhibin"},{"first_name":"Manuel","full_name":"Corva, Manuel","last_name":"Corva"},{"full_name":"Amin, Hatem M. A.","last_name":"Amin","first_name":"Hatem M. A."},{"full_name":"Blanc, Niclas","last_name":"Blanc","first_name":"Niclas"},{"id":"116779","full_name":"Linnemann, Julia","last_name":"Linnemann","orcid":"0000-0001-6883-5424","first_name":"Julia"},{"last_name":"Tschulik","full_name":"Tschulik, Kristina","first_name":"Kristina"}],"doi":"10.3390/ijms222313137","main_file_link":[{"open_access":"1"}],"publication_identifier":{"issn":["1422-0067"]},"publication_status":"published","intvolume":"        22","citation":{"apa":"Liu, Z., Corva, M., Amin, H. M. A., Blanc, N., Linnemann, J., &#38; Tschulik, K. (2021). Single Co<sub>3</sub>O<sub>4</sub> Nanocubes Electrocatalyzing the Oxygen Evolution Reaction: Nano-Impact Insights into Intrinsic Activity and Support Effects. <i>International Journal of Molecular Sciences</i>, <i>22</i>(23), Article 13137. <a href=\"https://doi.org/10.3390/ijms222313137\">https://doi.org/10.3390/ijms222313137</a>","mla":"Liu, Zhibin, et al. “Single Co<sub>3</sub>O<sub>4</sub> Nanocubes Electrocatalyzing the Oxygen Evolution Reaction: Nano-Impact Insights into Intrinsic Activity and Support Effects.” <i>International Journal of Molecular Sciences</i>, vol. 22, no. 23, 13137, MDPI AG, 2021, doi:<a href=\"https://doi.org/10.3390/ijms222313137\">10.3390/ijms222313137</a>.","bibtex":"@article{Liu_Corva_Amin_Blanc_Linnemann_Tschulik_2021, title={Single Co<sub>3</sub>O<sub>4</sub> Nanocubes Electrocatalyzing the Oxygen Evolution Reaction: Nano-Impact Insights into Intrinsic Activity and Support Effects}, volume={22}, DOI={<a href=\"https://doi.org/10.3390/ijms222313137\">10.3390/ijms222313137</a>}, number={2313137}, journal={International Journal of Molecular Sciences}, publisher={MDPI AG}, author={Liu, Zhibin and Corva, Manuel and Amin, Hatem M. A. and Blanc, Niclas and Linnemann, Julia and Tschulik, Kristina}, year={2021} }","short":"Z. Liu, M. Corva, H.M.A. Amin, N. Blanc, J. Linnemann, K. Tschulik, International Journal of Molecular Sciences 22 (2021).","ama":"Liu Z, Corva M, Amin HMA, Blanc N, Linnemann J, Tschulik K. Single Co<sub>3</sub>O<sub>4</sub> Nanocubes Electrocatalyzing the Oxygen Evolution Reaction: Nano-Impact Insights into Intrinsic Activity and Support Effects. <i>International Journal of Molecular Sciences</i>. 2021;22(23). doi:<a href=\"https://doi.org/10.3390/ijms222313137\">10.3390/ijms222313137</a>","chicago":"Liu, Zhibin, Manuel Corva, Hatem M. A. Amin, Niclas Blanc, Julia Linnemann, and Kristina Tschulik. “Single Co<sub>3</sub>O<sub>4</sub> Nanocubes Electrocatalyzing the Oxygen Evolution Reaction: Nano-Impact Insights into Intrinsic Activity and Support Effects.” <i>International Journal of Molecular Sciences</i> 22, no. 23 (2021). <a href=\"https://doi.org/10.3390/ijms222313137\">https://doi.org/10.3390/ijms222313137</a>.","ieee":"Z. Liu, M. Corva, H. M. A. Amin, N. Blanc, J. Linnemann, and K. Tschulik, “Single Co<sub>3</sub>O<sub>4</sub> Nanocubes Electrocatalyzing the Oxygen Evolution Reaction: Nano-Impact Insights into Intrinsic Activity and Support Effects,” <i>International Journal of Molecular Sciences</i>, vol. 22, no. 23, Art. no. 13137, 2021, doi: <a href=\"https://doi.org/10.3390/ijms222313137\">10.3390/ijms222313137</a>."},"_id":"62805","department":[{"_id":"985"}],"user_id":"116779","article_number":"13137","article_type":"original","extern":"1","type":"journal_article","status":"public","publisher":"MDPI AG","date_created":"2025-12-03T15:35:52Z","title":"Single Co<sub>3</sub>O<sub>4</sub> Nanocubes Electrocatalyzing the Oxygen Evolution Reaction: Nano-Impact Insights into Intrinsic Activity and Support Effects","quality_controlled":"1","issue":"23","year":"2021","keyword":["electrocatalysis","oxygen evolution reaction","cobalt spinel","single-entity electrochemistry"],"language":[{"iso":"eng"}],"publication":"International Journal of Molecular Sciences","abstract":[{"lang":"eng","text":"Single-entity electrochemistry allows for assessing electrocatalytic activities of individual material entities such as nanoparticles (NPs). Thus, it becomes possible to consider intrinsic electrochemical properties of nanocatalysts when researching how activity relates to physical and structural material properties. Conversely, conventional electrochemical techniques provide a normalized sum current referring to a huge ensemble of NPs constituting, along with additives (e.g., binders), a complete catalyst-coated electrode. Accordingly, recording electrocatalytic responses of single NPs avoids interferences of ensemble effects and reduces the complexity of electrocatalytic processes, thus enabling detailed description and modelling. Herein, we present insights into the oxygen evolution catalysis at individual cubic Co3O4 NPs impacting microelectrodes of different support materials. Simulating diffusion at supported nanocubes, measured step current signals can be analyzed, providing edge lengths, corresponding size distributions, and interference-free turnover frequencies. The provided nano-impact investigation of (electro-)catalyst-support effects contradicts assumptions on a low number of highly active sites."}]}]