Carbohydrate Co-Solutes Stabilize Collagen Triple Helices

NOMURA, Kota; Tomáš FIALA a Helma WENNEMERS. Carbohydrate Co-Solutes Stabilize Collagen Triple Helices. Chembiochem. WEINHEIM: WILEY-VCH, 2024, roč. 25, č. 5, 5 s. ISSN 1439-4227. Dostupné z: https://doi.org/10.1002/cbic.202300860.

Základní údaje

Originální název

Carbohydrate Co-Solutes Stabilize Collagen Triple Helices

Autoři

NOMURA, Kota; Tomáš FIALA ORCID a Helma WENNEMERS

Vydání

Chembiochem, WEINHEIM, WILEY-VCH, 2024, 1439-4227

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Další údaje

Typ výsledku

Článek v odborném periodiku

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 2.800

Označené pro přenos do RIV

Ne

DOI

https://doi.org/10.1002/cbic.202300860

Klíčová slova anglicky

collagen; carbohydrates; peptides; proline; trehalose

Štítky

ne MU, ne RIV

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Anotace

V originále

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 degrees 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.