Insight into Protein-Polymer Conjugate Relaxation Dynamics: The Importance of Polymer Grafting.
dynamical transition
hydration water
neutron scattering
properties of protein-polymer conjugates
protein dynamics
Journal
Macromolecular bioscience
ISSN: 1616-5195
Titre abrégé: Macromol Biosci
Pays: Germany
ID NLM: 101135941
Informations de publication
Date de publication:
06 2020
06 2020
Historique:
received:
29
11
2019
revised:
27
03
2020
pubmed:
15
4
2020
medline:
3
6
2021
entrez:
15
4
2020
Statut:
ppublish
Résumé
The bio and chemical physics of protein-polymer conjugates are related to parameters that characterize each component. With this work, it is intended to feature the dynamical properties of the protein-polymer conjugate myoglobin (Mb)-poly(ethyl ethylene phosphate), in the ps and ns time scales, in order to understand the respective roles of the protein and of the polymer size in the dynamics of the conjugate. Elastic and quasi-elastic neutron scattering is performed on completely hydrogenated samples with variable number of polymer chains covalently attached to the protein. The role of the polymer length in the protein solvation and internal dynamics is investigated using two conjugates formed by polymers of different molecular weight. It is confirmed that the flexibility of the complex increases with the number of grafted polymer chains and that a sharp dynamical transition appears when either grafting density or polymer molecular weight are high. It is shown that protein size is crucial for the polymer structural organization and interaction on the protein surface and it is established that the glass properties of the polymer change upon conjugation. The results give a better insight of the equivalence of the polymer coating and the role of water on the surface of proteins.
Identifiants
pubmed: 32285628
doi: 10.1002/mabi.201900410
doi:
Substances chimiques
Myoglobin
0
Polyesters
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e1900410Informations de copyright
© 2020 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Références
I. Cobo, M. Li, B. S. Sumerlin, S. Perrier, Nat. Mater. 2015, 14, 143.
A. N. Zelikin, C. Ehrhardt, A. M. Healy, Nat. Chem. 2016, 8, 997.
Y. Hou, H. Lu, Bioconjugate Chem. 2019, 30, 1604.
E. P. DeBenedictis, E. Hamed, S. Keten, ACS Nano 2016, 10, 2259.
A. J. Russell, S. L. Baker, C. M. Colina, C. A. Figg, J. L. Kaar, K. Matyjaszewski, A. Simakova, B. S. Sumerlin, AIChE J. 2018, 64, 3230.
K. N. Bauer, H. T. Tee, M. M. Velencoso, F. R. Wurm, Prog. Polym. Sci. 2017, 73, 61.
D. Russo, M. Plazanet, J. Teixeira, M. Moulin, M. Härtlein, F. R. Wurm, T. Steinbach, Biomacromolecules 2016, 17, 141.
T. Steinbach, G. Becker, A. Spiegel, T. Figueiredo, D. Russo, F. R. Wurm, Macromol. Biosci. 2017,17, 1600377.
T. Steinbach, F. R. Wurm, Biomacromolecules 2016, 17, 3338.
J. Simon, T. Wolf, K. Klein, K. Landfester, F. R. Wurm, V. Mailänder, Angew. Chem., Int. Ed. 2018, 57, 5548.
F. Zhang, J. A. Smolen, S. Zhang, R. Li, P. N. Shah, S. Cho, H. Wang, J. E. Raymond, C. L. Cannon, K. L. Wooley, Nanoscale 2015, 7, 2265.
S. M. Ryan, G. Mantovani, X. Wang, D. M. Haddleton, D. J. Brayden, Expert Opin. Drug Delivery 2008, 5, 371.
J. Wang, H. Q. Mao, K. W. Leong, J. Am. Chem. Soc. 2001, 123, 9480.
J. Müller, K. N. Bauer, D. Prozeller, J. Simon, V. Mailänder, F. R. Wurm, S. Winzen, K. Landfester, Biomaterials 2017, 115, 1.
T. Steinbach, S. Ritz, F. R. Wurm, ACS Macro Lett. 2014, 3, 244.
C. Pelosi, C. Duce, D. Russo, M. R. Tiné, F. R. Wurm, Eur. Polym. J. 2018, 108, 357.
D. Russo, A. de Angelis, A. Paciaroni, B. Frick, N. de Sousa, F. R. Wurm, J. Teixeira, Langmuir 2019, 35, 2674.
D. Russo, A. de Angelis, C. J. Garvey, F. R. Wurm, M.-S. Appavou, S. Prevost, Biomacromolecules 2019, 20, 1944.
H. Murata, C. S. Cummings, R. R. Koepsel, A. J. Russell, Biomacromolecules 2013, 14, 1919.
M. Lucius, R. Falatach, C. McGlone, K. Makaroff, A. Danielson, C. Williams, J. C. Nix, D. Konkolewicz, R. C. Page, J. A. Berberich, Biomacromolecules 2016, 17, 1123.
C. le Cœur, S. Combet, G. Carrot, P. Busch, J. Teixeira, S. Longeville, Langmuir 2015, 31, 8402.
D. Russo, M. D. Lambreva, C. A. Simionesco, P. Sebban, G. Rea, Biophys. J. 2019, 116, 1759.
D. Russo, J. Teixeira, J. Ollivier, J. Chem. Phys. 2009, 130, 235101.
B. Frick, J. Combet, L. Van Eijck, Nucl. Instrum. Methods Phys. Res., Sect. A 2012, 669, 7.
D. Russo, J. Ollivier, J. Teixeira, Phys. Chem. Chem. Phys. 2008, 10, 4968.
D. Russo, J. R. D. Copley, J. Ollivier, J. Teixeira, J. Mol. Struct. 2010, 972, 81.
L. Hong, N. Smolin, B. Lindner, A. P. Sokolov, J. C. Smith, Phys. Rev. Lett. 2011, 107, 148102.
D. Russo, J. Teixeira, unpublished.
M. Fomina, G. Schirò, A. Cupane, Biophys. Chem. 2014, 185, 25.
W. Doster, S. Cusack, W. Petry, Nature 1989, 337, 754.
A. Paciaroni, S. Cinelli, E. Cornicchi, A. de Francesco, G. Onori, Chem. Phys. Lett. 2005, 410, 400.
A. L. Tournier, J. C. Smith, Phys. Rev. Lett. 2003, 91, 208106.
J. Pérez, J. M. Zanotti, D. Durand, Biophys. J. 1999, 77, 454.
B. Frick, E. Mamontov, L. Van Eijck, T. Seydel, Z. Phys. Chem. 2010, 24, 33.
M. Hennig, B. Frick, T. Seydel, J. Appl. Crystallogr. 2011, 44, 467.
M. Appel, B. Frick, A. Magerl, Phys. B 2019, 562, 6.
M. Appel, B. Frick, A. Magerl, Sci. Rep. 2018, 8, 13580.
J. Ollivier, H. Mutka, J. Phys. Soc. Jpn. 2011, 80, SB003.
J. Ollivier, H. Mutka, L. Didier, Neutron News 2010, 21, 22.
D. Yu, R. Mole, T. Noakes, S. Kennedy, R. Robinson, J. Phys. Soc. Jpn. 2013, 82, SA027.
D. Yu, R. A. Mole, G. J. Kearley, EPJ Web Conf., 2015, 83, 03019.
R. A. Mole, D. Yu, Neutron News 2016, 27, 33.