Photocatalytic proton reduction is a promising way to produce dihydrogen (H-2) in a clean and sustainable manner, and mimicking nature by immobilising proton reduction catalysts and... Show morePhotocatalytic proton reduction is a promising way to produce dihydrogen (H-2) in a clean and sustainable manner, and mimicking nature by immobilising proton reduction catalysts and photosensitisers on liposomes is an attractive approach for biomimetic solar fuel production in aqueous solvents. Current photocatalytic proton reduction systems on liposomes are, however, limited by the stability of the catalyst. To overcome this problem, a new alkylated cobalt(II) polypyridyl complex (CoC12) was synthesised and immobilised on the lipid bilayer of liposomes, and its performance was studied in a photocatalytic system containing an alkylated ruthenium photosensitiser (RuC12) and a 1 : 1 mixture of sodium ascorbate and tris-2-carboxyethylphosphine hydrochloride as sacrificial electron donors. Several parameters (concentration of CoC12 and RuC12, pH, membrane composition) were changed to optimise the turnover number for H-2 production. Overall, CoC12 was found to be photostable and the optimised turnover number (161) was limited only by the decomposition of the ruthenium-based photosensitiser. Show less
Labra Munoz, J.A.; Reuver, A. de; Koeleman, F.; Huber, M.I.; Zant, H.S.J. van der 2022
We report on the fabrication of single-electron devices based on horse-spleen ferritin particles. At low temperatures the current vs. voltage characteristics are stable, enabling the acquisition of... Show moreWe report on the fabrication of single-electron devices based on horse-spleen ferritin particles. At low temperatures the current vs. voltage characteristics are stable, enabling the acquisition of reproducible data that establishes the Coulomb blockade as the main transport mechanism through them. Excellent agreement between the experimental data and the Coulomb blockade theory is demonstrated. Single-electron charge transport in ferritin, thus, establishes a route for further characterization of their, e.g., magnetic, properties down to the single-particle level, with prospects for electronic and medical applications. Show less
Miao, Q.; Zurlo, E.; Bruin, D. de; Wondergem, J.A.J.; Skinner, S.P.; Timmer, M.; ... ; Huber, M.I. 2021
CORRIGENDUM Q. Miao, E. Zurlo, D. de Bruin, J. A. J. Wondergem, S. P. Skinner, M. Timmer, A. Blok, D. Heinrich, M. Overhand, M. Huber,* M. Ubbink* 17128–17133 A Two-Armed Probe for In-Cell DEER... Show moreCORRIGENDUM Q. Miao, E. Zurlo, D. de Bruin, J. A. J. Wondergem, S. P. Skinner, M. Timmer, A. Blok, D. Heinrich, M. Overhand, M. Huber,* M. Ubbink* 17128–17133 A Two-Armed Probe for In-Cell DEER Measurements on Proteins Chem. Eur. J., 2020, 26 DOI: 10.1002/chem.202002743 All authors have agreed that Dr. Simon P. Skinner has made a significant contribution to this work by performing experiments and analyzing data and that his name should have been included in the list of authors. The corrected list of authors therefore reads: Dr. Qing Miao, Dr. Enrico Zurlo, Donny de Bruin, Joeri A. J. Wondergem, Dr. Simon P. Skinner, Monika Timmer, Anneloes Blok, Prof. Dr. Doris Heinrich, Dr. Mark Overhand, Dr. Martina Huber, Prof. Dr. Marcellus Ubbink The relevant affiliations for Dr. Skinner are (1) Leiden Institute of Chemistry, Gorlaeus Laboratories, Leiden University, Einsteinweg 55, 2333, CC Leiden, The Netherlands and (2) School of Molecular and Cellular Biology and Astbury Centre, University of Leeds, Leeds LS2 9JT, UK. The Acknowledgement section should not contain the sentence “and Dr. Simon Skinner for CLaNP5 labeled T4lys NMR data. Show less
Amyloid oligomers are suspected as toxic agents in neurodegenerative disease, and are transient and often heterogeneous, making them difficult to detect. Here we show an approach to track the... Show moreAmyloid oligomers are suspected as toxic agents in neurodegenerative disease, and are transient and often heterogeneous, making them difficult to detect. Here we show an approach to track the development of amyloid oligomers in situ by room temperature, continuous wave (cw) 9 and 95 GHz EPR. Three amyloid peptides with the 2,2,6,6-tetramethyl-N-oxyl-4-amino-4-carboxylic acid (TOAC) spin label were synthesized by solid phase peptide synthesis: T0EZ (TKVKVLGDVIEVGG) with TOAC (T) at the N-terminus, T5EZ with TOAC in the middle (KVKVTGDVIEVG) and T12EZ with TOAC at the C-terminus (KVKVLGDVIEVTG). These sequences are derived from the K11V (KVKVLGDVIEV) amyloid peptide, which self-aggregates to oligomers with a β-sheet configuration (A. Laganowsky, et al., Science, 2012, 335, 1228-1231). To monitor oligomerization, the rotational correlation time (τr) is measured by cw-EPR. For the backbone-fixed TOAC label that is devoid of local mobility τr should reflect the rotation and thereby the size of the peptide, resp. oligomer. For T5EZ a good match between the measured τr and the size of the peptide is obtained, showing the validity of the approach. One of the three peptides (T0EZ) aggregates (circular dichroism), whereas the other two do not. Since also the respective MTSL (S-(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl methanesulfonothioate) labelled peptides fail to aggregate, molecular crowding due to the label, rather than the helix-inducing properties of TOAC, seems to be responsible. Following in situ oligomer formation of T0EZ by the change in rotational correlation time, two oligomers are observed, a 5-6 mer and a 15-18 mer. The EPR approach, particularly 95 GHz EPR, enables following oligomerization of one monomer at a time, suggesting that the cw-EPR approach presented is a novel tool to follow amyloid oligomerization with high resolution. Show less
Bulk, M.; Weerd, L. van der; Breimer, W.; Lebedev, N.; Webb, A.; Goeman, J.J.; ... ; Bossoni, L. 2018
The amyloid β (A β) peptide is important in the context of Alzheimer's disease, since it is one of the major components of the fibrils that constitute amyloid plaques. Agents that can influence... Show moreThe amyloid β (A β) peptide is important in the context of Alzheimer's disease, since it is one of the major components of the fibrils that constitute amyloid plaques. Agents that can influence fibril formation are important, and of those, membrane mimics are particularly relevant, because the hydrophobic part of A β suggests a possible membrane activity of the peptide. We employed spin-label EPR to investigate the aggregation process of A β1-40 in the presence of the sodium dodecyl sulfate (SDS) detergent as a membrane-mimicking agent. In this work, the effect of SDS on A β is studied using two positions of spin label, the N-terminus and position 26. By comparing the two label positions, the effect of local mobility of the spin label is eliminated, revealing A β aggregation in the SDS concentration regime below the critical micelle concentration (CMC). We demonstrate that, at low SDS concentrations, the N-terminus of A β participates in the solubilization, most likely by being located at the particle-water interface. At higher SDS concentrations, an SDS-solubilized state that is a precursor to the one A β/micelle state above the CMC of SDS prevails. We propose that A β is membrane active and that aggregates include SDS. This study reveals the unique potential of EPR in studying A β aggregation in the presence of detergent. Show less
