Investigation of the structure of protein–polymer conjugates in solution reveals the impact of protein deuteration and the size of the polymer on its thermal stability

Author:

Russo Daniela1ORCID,Di Venere Almerinda2,Wurm Frederik R.3,Moulin Martine4,Härtlein Michael4,Garvey Christopher J.5,Teixeira José6

Affiliation:

1. CNR‐IOM (Italy) & Institut Laue Langevin Grenoble France

2. Department of Experimental Medicine Tor Vergata University of Rome Rome Italy

3. Sustainable Polymer Chemistry, Department of Molecules and Materials, MESA+ Institute of Nanotechnology, Faculty of Science and Technology University of Twente Enschede The Netherlands

4. ILL Deuteration Laboratory Partnership for Structural Biology Grenoble France

5. Forschungsneutronenquelle Heinz Maier‐Leibnitz FRM II and Physik Department E13 Technische Universität München Garching Germany

6. Laboratoire Léon Brillouin (CEA/CNRS) CEA Saclay Gif‐sur‐Yvette France

Abstract

AbstractThe conjugation of proteins with polymers offers immense biotechnological potential by creating novel macromolecules. This article presents experimental findings on the structural properties of maltose‐binding protein (MBP) conjugated with linear biodegradable polyphosphoester polymers with different molecular weights. We studied isotopic effects on both proteins and polymers. Circular dichroism and fluorescence spectroscopy and small‐angle neutron scattering reveal that the conjugation process destabilizes the protein, affecting the secondary more than the tertiary structure, even at room temperature, and that the presence of two domains in the MBP may contribute to its observed instability. Notably, unfolding temperatures differ between native MBP and the conjugates. In particular, this study sheds light on the complex interplay of factors such as the deuteration influencing protein stability and conformational changes in the conjugation processes. The perdeuteration influences the hydrogen bond network and hydrophobic interactions in the case of the MBP protein. The perdeuteration of the protein influences the hydrogen bond network and hydrophobic interactions. This is evident in the decreased thermal stability of deuterated MBP protein, in the conjugate, especially with high‐molecular‐mass polymers.

Funder

French Infrastructure for Integrated Structural Biology

Publisher

Wiley

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