ArticleACS omega2024
Tyrosine Mutation in the Characteristic Motif of the Amorphous Region of Spidroin for Self-Assembly Capability Enhancement.
Article in ACS omega, 2024. 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.
- Phosphate- and pH-dependent self-assembly of recombinant spider silk proteins.Protein science : a publication of the Protein Society · 2026Article
- An engineered self-cleavage fusion system for the production of chimaera spider silk proteins.BMC biotechnology · 2025Article
- Elasticity Anisotropy ofBiomacromolecules · 2025Article
- Artificial Spidroin Nanogenerator-Based Articulus Wound Dressing.ChemistryOpen · 2025Article
- Progress in Multiscale Modeling of Silk Materials.Biomacromolecules · 2024Review
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Authors and funding
8 authors.
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Abstract
Spidroin, with robust mechanical performance and good biocompatibility, could fulfill broad applications in material science and biomedical fields. Development of miniature spidroin has made abundant fiber production economically feasible, but the mechanical properties of artificial silk still fall short of natural silk. The mechanism behind mechanical properties of spidroin usually focuses on β-microcrystalline regions; the effect of amorphous regions was barely studied. In this study, residue tyrosines (Y) were designed to replace asparagine (N)/glutamic acid (Q) in the characteristic motifs (GGX)n in amorphous regions for performance enhancement of spidroin; the mutants presented lower free energy and significantly exhibited stronger van der Waals and electrostatic interactions, which might result from π-π stacking interactions between the phenyl rings in the side chain of tyrosine. Additionally, the soluble expressions of wild-type spidroin and mutant spidroin were achieved when heterologously expressed in
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