The role of disaccharides for protein–protein interactions – a SANS study
Artikel i vetenskaplig tidskrift, 2019

The disaccharide trehalose has shown outstanding anti-aggregation properties for proteins, which are highly important for the possibility to treat neurodegenerative diseases, such as Alzheimer's and Huntington's disease. However, the role and mechanism of trehalose for such stabilising effects are still largely unknown, partly because a direct structural picture of how trehalose organises around proteins in an aqueous system is missing. Here we compare small-angle neutron scattering (SANS) data on myoglobin in aqueous solutions of either sucrose or trehalose, in order to investigate their effect on protein-protein interactions. We find that both trehalose and sucrose induces a well-defined protein-protein distance, which could explain why these inhibit protein-protein interactions and associated protein aggregation. It does not however explain the superior anti-aggregation effect of trehalose and suggests that the local solvent structures are highly important for explaining the protein stabilisation mechanism. In a broader perspective, these findings are important for understanding the role of sugars in biological stabilisation, and could provide a structural explanation for why trehalose is a promising candidate for the treatment of neurodegenerative and other protein aggregation related diseases.

disaccharides

protein stabilisation

small-angle neutron scattering

Protein aggregation

Författare

Christoffer Olsson

Chalmers, Fysik, Biologisk fysik

Jan Swenson

Chalmers, Fysik, Biologisk fysik

Molecular Physics

0026-8976 (ISSN) 1362-3028 (eISSN)

Vol. 117 22 3408-3416

Struktur och dynamik i mjuka och biologiska material. I & II

Vetenskapsrådet (VR), 2016-01-01 -- 2019-12-31.

Vetenskapsrådet (VR), 2012-01-01 -- 2015-12-31.

Ämneskategorier

Astronomi, astrofysik och kosmologi

Atom- och molekylfysik och optik

Teoretisk kemi

DOI

10.1080/00268976.2019.1640400

Mer information

Senast uppdaterat

2019-12-11