ArticleNature communications2022
Extensible and self-recoverable proteinaceous materials derived from scallop byssal thread.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 26 citations in OpenAlex.
- Recombinant Proteins: A Molecular Tool to Understand Marine Adhesion and to Advance Biomaterials.Advanced healthcare materials · 2026Review
- Genome-wide Identification and Expression Profiling Indicate the Segon Gene Family Diversity and their Possible Role in Shell Formation in Oysters.Marine biotechnology (New York, N.Y.) · 2025Article
- An Overview on the Adhesion Mechanisms of Typical Aquatic Organisms and the Applications of Biomimetic Adhesives in Aquatic Environments.International journal of molecular sciences · 2024Review
- Multifunctionality in Nature: Structure-Function Relationships in Biological Materials.Biomimetics (Basel, Switzerland) · 2023Review
- Aqueous spinning of robust, self-healable, and crack-resistant hydrogel microfibers enabled by hydrogen bond nanoconfinement.Nature communications · 2023Article
Corrections and comments
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Authors and funding
18 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Biologically derived and biologically inspired fibers with outstanding mechanical properties have found attractive technical applications across diverse fields. Despite recent advances, few fibers can simultaneously possess high-extensibility and self-recovery properties especially under wet conditions. Here, we report protein-based fibers made from recombinant scallop byssal proteins with outstanding extensibility and self-recovery properties. We initially investigated the mechanical properties of the native byssal thread taken from scallop Chlamys farreri and reveal its high extensibility (327 ± 32%) that outperforms most natural biological fibers. Combining transcriptome and proteomics, we select the most abundant scallop byssal protein type 5-2 (Sbp5-2) in the thread region, and produce a recombinant protein consisting of 7 tandem repeat motifs (rTRM7) of the Sbp5-2 protein. Applying an organic solvent-enabled drawing process, we produce bio-inspired extensible rTRM7 fiber with high-extensibility (234 ± 35%) and self-recovery capability in wet condition, recapitulating the hierarchical structure and mechanical properties of the native scallop byssal thread. We further show that the mechanical properties of rTRM7 fiber are highly regulated by hydrogen bonding and intermolecular crosslinking formed through disulfide bond and metal-carboxyl coordination. With its outstanding mechanical properties, rTRM7 fiber can also be seamlessly integrated with graphene to create motion sensors and electrophysiological signal transmission electrode.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.