Journal Article

IMPULSE-2024-00189

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png 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

Russo, D. (Corresponding author) ; Di Venere, A. ; Wurm, F. R. ; Moulin, M. ; Härtlein, M. ; Garvey, C. J.MLZ* ; Teixeira, J.

2024
Protein Society Bethesda, Md.

Please use a persistent id in citations: doi:10.1002/pro.5032

Abstract: The 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.

Keyword(s): Polymers, Soft Nano Particles and Proteins (1st) ; Soft Condensed Matter (2nd)

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Contributing Institute(s):

1. SOFTMATTER (SOFTMATTER)
2. TOFTOF (TOFTOF)

Experiment(s):

1. Measurement at external facility

Appears in the scientific report 2024

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Database coverage:
; BIOSIS Previews ; Biological Abstracts ; Clarivate Analytics Master Journal List ; Current Contents - Life Sciences ; DEAL Wiley ; Essential Science Indicators ; IF >= 5 ; JCR ; PubMed Central ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection

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