Marine Structural Protein Stability Induced by Hofmeister Salt Annealing and Enzymatic Cross-Linking.
ACS Biomater Sci Eng
; 6(10): 5519-5526, 2020 10 12.
Article
em En
| MEDLINE
| ID: mdl-33320559
ABSTRACT
The Humboldt squid is one of the fiercest marine predators thanks in part to its sucker ring teeth that are biopolymer blends of a protein isoform family called suckerin with compression strength that rivals silkworm silk. Here, we focus on the popular suckerin-12 isoform to understand what makes the secondary structure of this biopolymer different in water and the potential role of diverse physical and chemical cross-linkings. By choosing a salt post-treatment, in accordance with the Hofmeister series, we achieved film stability with salt annealing that is comparable to chemical cross-links. By correlating the film morphology with the protein secondary structure changes, suckerin-12 films were shown to contract upon treatment with kosmotropic salts and exhibited increased stability in water. These changes are related to the rearrangement of suckerin-12 secondary structure from random coils and helices to ß-sheets. Overall, understanding secondary structure changes caused by aqueous and ionic environments can be instructive for the tuning of the suckerin film sclerotization, its conversion to a tough biological material, and to ultimately produce the natural squid sucker ring teeth.
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Base de dados:
MEDLINE
Assunto principal:
Decapodiformes
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Seda
Limite:
Animals
Idioma:
En
Revista:
ACS Biomater Sci Eng
Ano de publicação:
2020
Tipo de documento:
Article
País de afiliação:
Estados Unidos