Open access
Date
2024-03-01Type
- Journal Article
ETH Bibliography
yes
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Abstract
Carbohydrates are common co-solutes for the stabilization of proteins. The effect of carbohydrate solutions on the stability of collagen, the most abundant protein in mammals, is, however, underexplored. In this work, we studied the thermal stability of collagen triple helices derived from a molecularly defined collagen model peptide (CMP), Ac-(Pro-Hyp-Gly)₇-NH₂, in solutions of six common mono- and disaccharides. We show that the carbohydrates stabilize the collagen triple helix in a concentration-dependent manner, with an increase of the melting temperature of up to 17 °C. In addition, we show that the stabilizing effect is similar for all studied sugars, including trehalose, which is otherwise considered a privileged bioprotectant. The results provided insight into the effects of sugar co-solutes on collagen triple helices and can aid the selection of storage environments for collagen-based materials and probes. Show more
Permanent link
https://doi.org/10.3929/ethz-b-000658775Publication status
publishedExternal links
Journal / series
ChemBioChemVolume
Pages / Article No.
Publisher
Wiley-VCHSubject
collagen; carbohydrates; peptides; proline; trehaloseFunding
207505 - Synthetic Collagen (SNF)
891009 - Collagen Origami (EC)
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ETH Bibliography
yes
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