Investigation into the Relaxation Dynamics of Polymer-Protein Conjugates Reveals Surprising Role of Polymer Solvation on Inherent Protein Flexibility - Laboratoire interdisciplinaire de Physique Accéder directement au contenu
Article Dans Une Revue Biomacromolecules Année : 2016

Investigation into the Relaxation Dynamics of Polymer-Protein Conjugates Reveals Surprising Role of Polymer Solvation on Inherent Protein Flexibility

Résumé

Fully biodegradable protein−polymer conjugates, namely, MBP-16 PMeEP (maltose binding protein−poly methyl-ethylene phosphonate), have been 17 investigated in order to understand the role of polymer solvation on protein 18 flexibility. Using elastic and quasi-elastic incoherent neutron scattering, in 19 combination with partially deuterated conjugate systems, we are able to disentangle 20 the polymer dynamics from the protein dynamics and meaningfully address the 21 coupling between both components. We highlight that, in the dry state, the protein− 22 polymer conjugates lack any dynamical transition in accordance with the generally 23 observed behavior for dry proteins. In addition, we observe a larger flexibility of the 24 conjugated protein, compared to the native protein, as well as a lack of polymer− 25 glass transition. Only upon water hydration does the conjugate recover its dynamical 26 transition, leading to the conclusion that exclusive polymer solvation is insufficient to 27 unfreeze fluctuations on the picosecond−nanosecond time scale in biomolecules. 28 Our results also confirm the established coupling between polymer and protein dynamics in the conjugate.

Dates et versions

hal-01583248 , version 1 (07-09-2017)

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Daniela R Russo, Marie Plazanet, Jose R Teixeira, Martine Moulin, Michael Härtlein, et al.. Investigation into the Relaxation Dynamics of Polymer-Protein Conjugates Reveals Surprising Role of Polymer Solvation on Inherent Protein Flexibility. Biomacromolecules, 2016, 17 (1), pp.141-147. ⟨10.1021/acs.biomac.5b01269⟩. ⟨hal-01583248⟩
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