Supramolecular Self-Assembly of Proteins Promoted by Hybrid Polyoxometalates.
hybrids
metal-oxo clusters
polyoxometalates
proteins
supramolecular assembly
Journal
Small (Weinheim an der Bergstrasse, Germany)
ISSN: 1613-6829
Titre abrégé: Small
Pays: Germany
ID NLM: 101235338
Informations de publication
Date de publication:
11 Jan 2024
11 Jan 2024
Historique:
received:
23
12
2023
medline:
12
1
2024
pubmed:
12
1
2024
entrez:
12
1
2024
Statut:
aheadofprint
Résumé
Controlling the formation of supramolecular protein assemblies and endowing them with new properties that can lead to novel functional materials is an important but challenging task. In this work, a new hybrid polyoxometalate is designed to induce controlled intermolecular bridging between biotin-binding proteins. Such bridging interactions lead to the formation of supramolecular protein assemblies incorporating metal-oxo clusters that go from several nanometers in diameter up to the micron range. Insights into the self-assembly process and the nature of the resulting biohybrid materials are obtained by a combination of Small Angle X-ray Scattering (SAXS), Transmission Electron Microscopy (TEM), and Dynamic Light Scattering (DLS), along with fluorescence, UV-vis, and Circular Dichroism (CD) spectroscopy. The formation of hybrid supramolecular assemblies is determined to be driven by biotin binding to the protein and electrostatic interactions between the anionic metal-oxo cluster and the protein, both of which also influence the stability of the resulting assemblies. As a result, the rate of formation, size, and stability of the supramolecular assemblies can be tuned by controlling the electrostatic interactions between the cluster and the protein (e.g., through varying the ionic strength of the solution), thereby paving the way toward biomaterials with tunable assembly and disassembly properties.
Identifiants
pubmed: 38213017
doi: 10.1002/smll.202312009
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2312009Subventions
Organisme : Research Foundation Flanders
Organisme : KU Leuven
Organisme : Onderzoeksraad, KU Leuven
ID : C14/19/076
Organisme : Vlaamse Overheid
Informations de copyright
© 2024 Wiley-VCH GmbH.
Références
B. J. G. E. Pieters, M. B. Van Eldijk, R. J. M. Nolte, J. Mecinovic, Chem. Soc. Rev. 2016, 45, 24.
S. L. Kuan, F. R. G. Bergamini, T. Weil, Chem. Soc. Rev. 2018, 47, 9069.
M. D. Shoulders, R. T. Raines, Annu. Rev. Biochem. 2009, 78, 929.
Y. Xu, J. Ye, H. Liu, E. Cheng, Y. Yang, W. Wang, M. Zhao, D. Zhou, D. Liu, R. Fang, Chem. Commun. 2008, 49.
X. Hu, A. Damjanovic, T. Ritz, K. Schulten, Proc. Natl. Acad. Sci. USA 1998, 95, 5935.
P. Sweeney, H. Park, M. Baumann, J. Dunlop, J. Frydman, R. Kopito, A. Mccampbell, G. Leblanc, A. Venkateswaran, A. Nurmi, R. Hodgson, Transl. Neurodegener. 2017, 6, 6.
G. Yang, L. Wu, G. Chen, M. Jiang, Chem. Commun. 2016, 52, 10595.
D. Y. W. Ng, Y. Wu, S. L. Kuan, T. Weil, Acc. Chem. Res. 2014, 47, 3471.
Y. Bai, Q. Luo, J. Liu, Chem. Soc. Rev. 2016, 45, 2756.
J. B. Bailey, L. Zhang, J. A. Chiong, S. Ahn, F. A. Tezcan, J. Am. Chem. Soc. 2017, 139, 8160.
P. A. Sontz, J. B. Bailey, S. Ahn, F. A. Tezcan, J. Am. Chem. Soc. 2015, 137, 11598.
N. Dotan, D. Arad, F. Frolow, A. Freeman, Angew. Chem., Int. Ed. 1999, 38, 2363.
F. Sakai, G. Yang, M. S. Weiss, Y. Liu, G. Chen, M. Jiang, Nat. Commun. 2014, 5, 4634.
P. Ringler, G. E. Schulz, Science 2003, 302, 106.
P. B. Crowley, Acc. Chem. Res. 2022, 55, 2019.
S. Van Dun, C. Ottmann, L.-G. Milroy, L. Brunsveld, J. Am. Chem. Soc. 2017, 139, 13960.
O. Livnah, E. A. Bayer, M. Wilchek, J. L. Sussman, Proc. Natl. Acad. Sci.,USA 1993, 90, 5076.
L. Pugliese, A. Coda, M. Malcovati, M. Bolognesi, J. Mol. Biol. 1993, 231, 698.
M. Wilchek, E. A. Bayer, Methods Enzymol. 1990, 184, 5.
N. M. Green, L. Konieczny, E. J. Toms, R. C. Valentine, Biochem. J. 1971, 125, 781.
N. M. Green, Methods Enzymol 1990, 184, 51.
D. S. Wilbur, P. M. Pathare, D. K. Hamlin, S. A. Weerawarna, Bioconjug. Chem. 1997, 8, 819.
S. Burazerovic, J. Gradinaru, J. Pierron, T. R. Ward, Angew. Chem., Int. Ed. 2007, 46, 5510.
K. K.-W. Lo, J. S.-Y. Lau, Inorg. Chem. 2007, 46, 700.
M. Skander, N. Humbert, J. Collot, J. Gradinaru, G. Klein, A. Loosli, J. Sauser, A. Zocchi, F. Gilardoni, T. R. Ward, J. Am. Chem. Soc. 2004, 126, 14411.
V. A. Zamolo, G. Modugno, E. Lubian, A. Cazzolaro, F. Mancin, L. Giotta, D. Mastrogiacomo, L. Valli, A. Saccani, S. Krol, M. Bonchio, M. Carraro, Front. Chem. 2018, 6, 278.
L. Olshansky, R. Huerta-Lavorie, A. I. Nguyen, J. Vallapurackal, A. Furst, T. D. Tilley, A. S. Borovik, J. Am. Chem. Soc. 2018, 140, 2739.
M. Stuckart, K. Y. Monakhov, Chem. Sci. 2019, 10, 4364.
T. Yamase, J. Mater. Chem. 2005, 15, 4773.
L. Vandebroek, H. Noguchi, K. Kamata, J. R. H. Tame, L. Van Meervelt, T. N. Parac-Vogt, A. R. D. Voet, Cryst. Growth Des. 2021, 21, 1307.
L. Vandebroek, H. Noguchi, K. Kamata, J. R. H. Tame, L. Van Meervelt, T. N. Parac-Vogt, A. R. D. Voet, Chem. Commun. 2020, 56, 11601.
J. M. Cameron, G. Guillemot, T. Galambos, S. S. Amin, E. Hampson, K. Mall Haidaraly, G. N. Newton, G. Izzet, Chem. Soc. Rev. 2022, 51, 293.
A. Blazevic, A. Rompel, Coord. Chem. Rev. 2016, 307, 42.
S. Lentink, D. E. Salazar Marcano, M. A. Moussawi, L. Vandebroek, L. Van Meervelt, T. N. Parac-Vogt, Faraday Discuss. 2023, 244, 21.
H. Soria-Carrera, E. Atrián-Blasco, J. M. De La Fuente, S. G. Mitchell, R. Martín-Rapún, Nanoscale 2022, 14, 5999.
D. E. Salazar Marcano, S. Lentink, M. A. Moussawi, T. N. Parac-Vogt, Inorg. Chem. 2021, 60, 10215.
M. S. Hosseini, S. Haghjooy Javanmard, L. Rafiei, A. A. Hariri, N. Dana, M. Rostami, Eurasian J. Med. Oncol. 2020, 4, 42.
The PyMOL Molecular Graphics System, Schrödinger, LLC, http://www.pymol.org, (accessed : April 2023).
M. Nyman, Coord. Chem. Rev. 2017, 352, 461.
I. S. Lee, J. R. Long, S. B. Prusiner, J. G. Safar, J. Am. Chem. Soc. 2005, 127, 13802.
A. Bijelic, A. Rompel, ChemTexts 2018, 4, 10.
I. Le Trong, Z. Wang, D. E. Hyre, T. P. Lybrand, P. S. Stayton, R. E. Stenkamp, Acta Crystallogr. Sect. D Biol. Crystallogr. 2011, 67, 813.
C. Zhang, T. He, A. Vedadghavami, A. G. Bajpayee, MethodsX 2020, 7, 100882.
J. R. Lakowicz, Principles of Fluorescence Spectroscopy, Springer US, Boston, MA 2006.
J. T. Vivian, P. R. Callis, Biophys. J. 2001, 80, 2093.
X.-Z. Feng, Z. Lin, L.-J. Yang, C. Wang, C.-L. Bai, Talanta 1998, 47, 1223.
V. Goovaerts, K. Stroobants, G. Absillis, T. N. Parac-Vogt, Phys. Chem. Chem. Phys. 2013, 15, 18378.
X. M. He, D. C. Carter, Nature 1992, 358, 209.
D. Malamud, J. W. Drysdale, Anal. Biochem. 1978, 86, 620.
O. Livnah, E. A. Bayer, M. Wilchek, J. L. Sussman, FEBS Lett. 1993, 328, 165.
J.-A. Farrera, I. Canal, P. Hidalgo-Fernández, M. L. Pérez-García, O. Huertas, F. J. Luque, Chem. - A Eur. J. 2008, 14, 2277.
N. M. Green, Biochem. J. 1965, 94, 23C.
N. J. Greenfield, Nat. Protoc. 2006, 1, 2876.
B. L. Li, M. I. Setyawati, L. Chen, J. Xie, K. Ariga, C.-T. Lim, S. Garaj, D. T. Leong, ACS Appl. Mater. Interfaces 2017, 9, 15286.
D. Y. W. Ng, J. Fahrer, Y. Wu, K. Eisele, S. L. Kuan, H. Barth, T. Weil, Adv. Healthcare Mater. 2013, 2, 1620.