---
_id: '50150'
abstract:
- lang: eng
text: 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.
article_number: '7226'
author:
- first_name: Patrick
full_name: Müller, Patrick
last_name: Müller
- first_name: Mergim
full_name: Meta, Mergim
last_name: Meta
- first_name: Jan Laurenz
full_name: Meidner, Jan Laurenz
last_name: Meidner
- first_name: Marvin
full_name: Schwickert, Marvin
last_name: Schwickert
- first_name: Jessica
full_name: Meyr, Jessica
last_name: Meyr
- first_name: Kevin
full_name: Schwickert, Kevin
last_name: Schwickert
- first_name: Christian
full_name: Kersten, Christian
last_name: Kersten
- first_name: Collin
full_name: Zimmer, Collin
last_name: Zimmer
- first_name: Stefan Josef
full_name: Hammerschmidt, Stefan Josef
last_name: Hammerschmidt
- first_name: Ariane
full_name: Frey, Ariane
last_name: Frey
- first_name: Albin
full_name: Lahu, Albin
last_name: Lahu
- first_name: Sergio
full_name: de la Hoz-Rodríguez, Sergio
last_name: de la Hoz-Rodríguez
- first_name: Laura
full_name: Agost-Beltrán, Laura
last_name: Agost-Beltrán
- first_name: Santiago
full_name: Rodríguez, Santiago
last_name: Rodríguez
- first_name: Kira
full_name: Diemer, Kira
last_name: Diemer
- first_name: Wilhelm
full_name: Neumann, Wilhelm
last_name: Neumann
- first_name: Florenci V.
full_name: Gonzàlez, Florenci V.
last_name: Gonzàlez
- first_name: Bernd
full_name: Engels, Bernd
last_name: Engels
- first_name: Tanja
full_name: Schirmeister, Tanja
last_name: Schirmeister
citation:
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. International Journal of Molecular Sciences. 2023;24(8).
doi:10.3390/ijms24087226
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., & Schirmeister, T. (2023). Investigation of the Compatibility
between Warheads and Peptidomimetic Sequences of Protease Inhibitors—A Comprehensive
Reactivity and Selectivity Study. International Journal of Molecular Sciences,
24(8), Article 7226. https://doi.org/10.3390/ijms24087226
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={10.3390/ijms24087226},
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}
}'
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.” International Journal of Molecular Sciences
24, no. 8 (2023). https://doi.org/10.3390/ijms24087226.
ieee: 'P. Müller et al., “Investigation of the Compatibility between Warheads
and Peptidomimetic Sequences of Protease Inhibitors—A Comprehensive Reactivity
and Selectivity Study,” International Journal of Molecular Sciences, vol.
24, no. 8, Art. no. 7226, 2023, doi: 10.3390/ijms24087226.'
mla: Müller, Patrick, et al. “Investigation of the Compatibility between Warheads
and Peptidomimetic Sequences of Protease Inhibitors—A Comprehensive Reactivity
and Selectivity Study.” International Journal of Molecular Sciences, vol.
24, no. 8, 7226, MDPI AG, 2023, doi:10.3390/ijms24087226.
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).
date_created: 2024-01-04T08:24:31Z
date_updated: 2024-01-05T12:59:32Z
doi: 10.3390/ijms24087226
intvolume: ' 24'
issue: '8'
keyword:
- Inorganic Chemistry
- Organic Chemistry
- Physical and Theoretical Chemistry
- Computer Science Applications
- Spectroscopy
- Molecular Biology
- General Medicine
- Catalysis
language:
- iso: eng
project:
- _id: '52'
name: 'PC2: Computing Resources Provided by the Paderborn Center for Parallel Computing'
publication: International Journal of Molecular Sciences
publication_identifier:
issn:
- 1422-0067
publication_status: published
publisher: MDPI AG
status: public
title: Investigation of the Compatibility between Warheads and Peptidomimetic Sequences
of Protease Inhibitors—A Comprehensive Reactivity and Selectivity Study
type: journal_article
user_id: '67287'
volume: 24
year: '2023'
...
---
_id: '46543'
abstract:
- lang: eng
text: 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.
article_number: '12808'
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
full_name: Li, Xinyang
last_name: Li
- first_name: Guido
full_name: Grundmeier, Guido
id: '194'
last_name: Grundmeier
- first_name: Denise J.
full_name: Erb, Denise J.
last_name: Erb
- first_name: Adrian
full_name: Keller, Adrian
id: '48864'
last_name: Keller
orcid: 0000-0001-7139-3110
citation:
ama: Pothineni BK, Kollmann S, Li X, Grundmeier G, Erb DJ, Keller A. Adsorption
of Ferritin at Nanofaceted Al2O3 Surfaces. International Journal of Molecular
Sciences. 2023;24(16). doi:10.3390/ijms241612808
apa: Pothineni, B. K., Kollmann, S., Li, X., Grundmeier, G., Erb, D. J., & Keller,
A. (2023). Adsorption of Ferritin at Nanofaceted Al2O3 Surfaces. International
Journal of Molecular Sciences, 24(16), Article 12808. https://doi.org/10.3390/ijms241612808
bibtex: '@article{Pothineni_Kollmann_Li_Grundmeier_Erb_Keller_2023, title={Adsorption
of Ferritin at Nanofaceted Al2O3 Surfaces}, volume={24}, DOI={10.3390/ijms241612808},
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} }'
chicago: Pothineni, Bhanu K., Sabrina Kollmann, Xinyang Li, Guido Grundmeier, Denise
J. Erb, and Adrian Keller. “Adsorption of Ferritin at Nanofaceted Al2O3 Surfaces.”
International Journal of Molecular Sciences 24, no. 16 (2023). https://doi.org/10.3390/ijms241612808.
ieee: 'B. K. Pothineni, S. Kollmann, X. Li, G. Grundmeier, D. J. Erb, and A. Keller,
“Adsorption of Ferritin at Nanofaceted Al2O3 Surfaces,” International Journal
of Molecular Sciences, vol. 24, no. 16, Art. no. 12808, 2023, doi: 10.3390/ijms241612808.'
mla: Pothineni, Bhanu K., et al. “Adsorption of Ferritin at Nanofaceted Al2O3 Surfaces.”
International Journal of Molecular Sciences, vol. 24, no. 16, 12808, MDPI
AG, 2023, doi:10.3390/ijms241612808.
short: B.K. Pothineni, S. Kollmann, X. Li, G. Grundmeier, D.J. Erb, A. Keller, International
Journal of Molecular Sciences 24 (2023).
date_created: 2023-08-16T10:52:25Z
date_updated: 2023-08-16T10:53:00Z
department:
- _id: '302'
doi: 10.3390/ijms241612808
intvolume: ' 24'
issue: '16'
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
publication_identifier:
issn:
- 1422-0067
publication_status: published
publisher: MDPI AG
status: public
title: Adsorption of Ferritin at Nanofaceted Al2O3 Surfaces
type: journal_article
user_id: '48864'
volume: 24
year: '2023'
...
---
_id: '30209'
abstract:
- lang: eng
text: 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.
author:
- first_name: Marcel
full_name: Hanke, Marcel
last_name: Hanke
- first_name: Niklas
full_name: Hansen, Niklas
last_name: Hansen
- first_name: Ruiping
full_name: Chen, Ruiping
last_name: Chen
- first_name: Guido
full_name: Grundmeier, Guido
last_name: Grundmeier
- first_name: Karim
full_name: Fahmy, Karim
last_name: Fahmy
- first_name: Adrian
full_name: Keller, Adrian
last_name: Keller
citation:
ama: Hanke M, Hansen N, Chen R, Grundmeier G, Fahmy K, Keller A. Salting-Out of
DNA Origami Nanostructures by Ammonium Sulfate. International Journal of Molecular
Sciences. 2022;23(5):2817. doi:10.3390/ijms23052817
apa: Hanke, M., Hansen, N., Chen, R., Grundmeier, G., Fahmy, K., & Keller, A.
(2022). Salting-Out of DNA Origami Nanostructures by Ammonium Sulfate. International
Journal of Molecular Sciences, 23(5), 2817. https://doi.org/10.3390/ijms23052817
bibtex: '@article{Hanke_Hansen_Chen_Grundmeier_Fahmy_Keller_2022, title={Salting-Out
of DNA Origami Nanostructures by Ammonium Sulfate}, volume={23}, DOI={10.3390/ijms23052817},
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} }'
chicago: 'Hanke, Marcel, Niklas Hansen, Ruiping Chen, Guido Grundmeier, Karim Fahmy,
and Adrian Keller. “Salting-Out of DNA Origami Nanostructures by Ammonium Sulfate.”
International Journal of Molecular Sciences 23, no. 5 (2022): 2817. https://doi.org/10.3390/ijms23052817.'
ieee: 'M. Hanke, N. Hansen, R. Chen, G. Grundmeier, K. Fahmy, and A. Keller, “Salting-Out
of DNA Origami Nanostructures by Ammonium Sulfate,” International Journal of
Molecular Sciences, vol. 23, no. 5, p. 2817, 2022, doi: 10.3390/ijms23052817.'
mla: Hanke, Marcel, et al. “Salting-Out of DNA Origami Nanostructures by Ammonium
Sulfate.” International Journal of Molecular Sciences, vol. 23, no. 5,
MDPI AG, 2022, p. 2817, doi:10.3390/ijms23052817.
short: M. Hanke, N. Hansen, R. Chen, G. Grundmeier, K. Fahmy, A. Keller, International
Journal of Molecular Sciences 23 (2022) 2817.
date_created: 2022-03-07T07:28:02Z
date_updated: 2022-03-07T07:29:27Z
department:
- _id: '302'
doi: 10.3390/ijms23052817
intvolume: ' 23'
issue: '5'
keyword:
- Inorganic Chemistry
- Organic Chemistry
- Physical and Theoretical Chemistry
- Computer Science Applications
- Spectroscopy
- Molecular Biology
- General Medicine
- Catalysis
language:
- iso: eng
page: '2817'
publication: International Journal of Molecular Sciences
publication_identifier:
issn:
- 1422-0067
publication_status: published
publisher: MDPI AG
status: public
title: Salting-Out of DNA Origami Nanostructures by Ammonium Sulfate
type: journal_article
user_id: '48864'
volume: 23
year: '2022'
...
---
_id: '32589'
abstract:
- lang: eng
text: 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.
author:
- first_name: Marcel
full_name: Hanke, Marcel
last_name: Hanke
- first_name: Niklas
full_name: Hansen, Niklas
last_name: Hansen
- first_name: Emilia
full_name: Tomm, Emilia
last_name: Tomm
- first_name: Guido
full_name: Grundmeier, Guido
id: '194'
last_name: Grundmeier
- first_name: Adrian
full_name: Keller, Adrian
id: '48864'
last_name: Keller
orcid: 0000-0001-7139-3110
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.
International Journal of Molecular Sciences. 2022;23(15):8547. doi:10.3390/ijms23158547
apa: Hanke, M., Hansen, N., Tomm, E., Grundmeier, G., & Keller, A. (2022). Time-Dependent
DNA Origami Denaturation by Guanidinium Chloride, Guanidinium Sulfate, and Guanidinium
Thiocyanate. International Journal of Molecular Sciences, 23(15),
8547. https://doi.org/10.3390/ijms23158547
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={10.3390/ijms23158547},
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} }'
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.” International Journal of Molecular Sciences
23, no. 15 (2022): 8547. https://doi.org/10.3390/ijms23158547.'
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,” International Journal of Molecular Sciences, vol. 23, no.
15, p. 8547, 2022, doi: 10.3390/ijms23158547.'
mla: Hanke, Marcel, et al. “Time-Dependent DNA Origami Denaturation by Guanidinium
Chloride, Guanidinium Sulfate, and Guanidinium Thiocyanate.” International
Journal of Molecular Sciences, vol. 23, no. 15, MDPI AG, 2022, p. 8547, doi:10.3390/ijms23158547.
short: M. Hanke, N. Hansen, E. Tomm, G. Grundmeier, A. Keller, International Journal
of Molecular Sciences 23 (2022) 8547.
date_created: 2022-08-08T06:39:20Z
date_updated: 2022-08-08T06:40:14Z
department:
- _id: '302'
doi: 10.3390/ijms23158547
intvolume: ' 23'
issue: '15'
keyword:
- Inorganic Chemistry
- Organic Chemistry
- Physical and Theoretical Chemistry
- Computer Science Applications
- Spectroscopy
- Molecular Biology
- General Medicine
- Catalysis
language:
- iso: eng
page: '8547'
publication: International Journal of Molecular Sciences
publication_identifier:
issn:
- 1422-0067
publication_status: published
publisher: MDPI AG
status: public
title: Time-Dependent DNA Origami Denaturation by Guanidinium Chloride, Guanidinium
Sulfate, and Guanidinium Thiocyanate
type: journal_article
user_id: '48864'
volume: 23
year: '2022'
...
---
_id: '22636'
abstract:
- lang: eng
text: 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.
author:
- first_name: Marcel
full_name: Hanke, Marcel
last_name: Hanke
- first_name: Yu
full_name: Yang, Yu
last_name: Yang
- first_name: Yuxin
full_name: Ji, Yuxin
last_name: Ji
- first_name: Guido
full_name: Grundmeier, Guido
id: '194'
last_name: Grundmeier
- first_name: Adrian
full_name: Keller, Adrian
id: '48864'
last_name: Keller
orcid: 0000-0001-7139-3110
citation:
ama: Hanke M, Yang Y, Ji Y, Grundmeier G, Keller A. Nanoscale Surface Topography
Modulates hIAPP Aggregation Pathways at Solid–Liquid Interfaces. International
Journal of Molecular Sciences. 2021;22:5142. doi:10.3390/ijms22105142
apa: Hanke, M., Yang, Y., Ji, Y., Grundmeier, G., & Keller, A. (2021). Nanoscale
Surface Topography Modulates hIAPP Aggregation Pathways at Solid–Liquid Interfaces.
International Journal of Molecular Sciences, 22, 5142. https://doi.org/10.3390/ijms22105142
bibtex: '@article{Hanke_Yang_Ji_Grundmeier_Keller_2021, title={Nanoscale Surface
Topography Modulates hIAPP Aggregation Pathways at Solid–Liquid Interfaces}, volume={22},
DOI={10.3390/ijms22105142},
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} }'
chicago: 'Hanke, Marcel, Yu Yang, Yuxin Ji, Guido Grundmeier, and Adrian Keller.
“Nanoscale Surface Topography Modulates HIAPP Aggregation Pathways at Solid–Liquid
Interfaces.” International Journal of Molecular Sciences 22 (2021): 5142.
https://doi.org/10.3390/ijms22105142.'
ieee: M. Hanke, Y. Yang, Y. Ji, G. Grundmeier, and A. Keller, “Nanoscale Surface
Topography Modulates hIAPP Aggregation Pathways at Solid–Liquid Interfaces,” International
Journal of Molecular Sciences, vol. 22, p. 5142, 2021.
mla: Hanke, Marcel, et al. “Nanoscale Surface Topography Modulates HIAPP Aggregation
Pathways at Solid–Liquid Interfaces.” International Journal of Molecular Sciences,
vol. 22, 2021, p. 5142, doi:10.3390/ijms22105142.
short: M. Hanke, Y. Yang, Y. Ji, G. Grundmeier, A. Keller, International Journal
of Molecular Sciences 22 (2021) 5142.
date_created: 2021-07-08T11:43:14Z
date_updated: 2022-01-06T06:55:37Z
department:
- _id: '302'
doi: 10.3390/ijms22105142
intvolume: ' 22'
language:
- iso: eng
page: '5142'
publication: International Journal of Molecular Sciences
publication_identifier:
issn:
- 1422-0067
publication_status: published
status: public
title: Nanoscale Surface Topography Modulates hIAPP Aggregation Pathways at Solid–Liquid
Interfaces
type: journal_article
user_id: '48864'
volume: 22
year: '2021'
...
---
_id: '62805'
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.
article_number: '13137'
article_type: original
author:
- first_name: Zhibin
full_name: Liu, Zhibin
last_name: Liu
- first_name: Manuel
full_name: Corva, Manuel
last_name: Corva
- first_name: Hatem M. A.
full_name: Amin, Hatem M. A.
last_name: Amin
- first_name: Niclas
full_name: Blanc, Niclas
last_name: Blanc
- first_name: Julia
full_name: Linnemann, Julia
id: '116779'
last_name: Linnemann
orcid: 0000-0001-6883-5424
- first_name: Kristina
full_name: Tschulik, Kristina
last_name: Tschulik
citation:
ama: 'Liu Z, Corva M, Amin HMA, Blanc N, Linnemann J, Tschulik K. Single Co3O4
Nanocubes Electrocatalyzing the Oxygen Evolution Reaction: Nano-Impact Insights
into Intrinsic Activity and Support Effects. International Journal of Molecular
Sciences. 2021;22(23). doi:10.3390/ijms222313137'
apa: 'Liu, Z., Corva, M., Amin, H. M. A., Blanc, N., Linnemann, J., & Tschulik,
K. (2021). Single Co3O4 Nanocubes Electrocatalyzing the
Oxygen Evolution Reaction: Nano-Impact Insights into Intrinsic Activity and Support
Effects. International Journal of Molecular Sciences, 22(23), Article
13137. https://doi.org/10.3390/ijms222313137'
bibtex: '@article{Liu_Corva_Amin_Blanc_Linnemann_Tschulik_2021, title={Single Co3O4
Nanocubes Electrocatalyzing the Oxygen Evolution Reaction: Nano-Impact Insights
into Intrinsic Activity and Support Effects}, volume={22}, DOI={10.3390/ijms222313137},
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} }'
chicago: 'Liu, Zhibin, Manuel Corva, Hatem M. A. Amin, Niclas Blanc, Julia Linnemann,
and Kristina Tschulik. “Single Co3O4 Nanocubes Electrocatalyzing
the Oxygen Evolution Reaction: Nano-Impact Insights into Intrinsic Activity and
Support Effects.” International Journal of Molecular Sciences 22, no. 23
(2021). https://doi.org/10.3390/ijms222313137.'
ieee: 'Z. Liu, M. Corva, H. M. A. Amin, N. Blanc, J. Linnemann, and K. Tschulik,
“Single Co3O4 Nanocubes Electrocatalyzing the Oxygen Evolution
Reaction: Nano-Impact Insights into Intrinsic Activity and Support Effects,” International
Journal of Molecular Sciences, vol. 22, no. 23, Art. no. 13137, 2021, doi:
10.3390/ijms222313137.'
mla: 'Liu, Zhibin, et al. “Single Co3O4 Nanocubes Electrocatalyzing
the Oxygen Evolution Reaction: Nano-Impact Insights into Intrinsic Activity and
Support Effects.” International Journal of Molecular Sciences, vol. 22,
no. 23, 13137, MDPI AG, 2021, doi:10.3390/ijms222313137.'
short: Z. Liu, M. Corva, H.M.A. Amin, N. Blanc, J. Linnemann, K. Tschulik, International
Journal of Molecular Sciences 22 (2021).
date_created: 2025-12-03T15:35:52Z
date_updated: 2025-12-03T16:52:35Z
department:
- _id: '985'
doi: 10.3390/ijms222313137
extern: '1'
intvolume: ' 22'
issue: '23'
keyword:
- electrocatalysis
- oxygen evolution reaction
- cobalt spinel
- single-entity electrochemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
oa: '1'
publication: International Journal of Molecular Sciences
publication_identifier:
issn:
- 1422-0067
publication_status: published
publisher: MDPI AG
quality_controlled: '1'
status: public
title: 'Single Co3O4 Nanocubes Electrocatalyzing the Oxygen
Evolution Reaction: Nano-Impact Insights into Intrinsic Activity and Support Effects'
type: journal_article
user_id: '116779'
volume: 22
year: '2021'
...