ArticleBiomacromolecules2017
Structural and Mechanical Roles for the C-Terminal Nonrepetitive Domain Become Apparent in Recombinant Spider Aciniform Silk.
Article in Biomacromolecules, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 27 citations in OpenAlex.
- Exploring the Unique Properties and Superior Schwann Cell Guiding Abilities of Spider Egg Sac Silk.ACS applied bio materials · 2025Article
- Post-spin Stretch Improves Mechanical Properties, Reduces Necking, and Reverts Effects of Aging in Biomimetic Artificial Spider Silk Fibers.ACS applied polymer materials · 2024Article
- Strategies for Making High-Performance Artificial Spider Silk Fibers.Advanced functional materials · 2024Review
- A recombinant chimeric spider pyriform-aciniform silk with highly tunable mechanical performance.Materials today. Bio · 2024Article
- Influence of Spider Silk Protein Structure on Mechanical and Biological Properties for Energetic Material Detection.Molecules (Basel, Switzerland) · 2024Review
- Influence of experimental methods on the mechanical properties of silk fibers: A systematic literature review and future road map.Biophysics reviews · 2023Review
- Bi-terminal fusion of intrinsically-disordered mussel foot protein fragments boosts mechanical strength for protein fibers.Nature communications · 2023Article
- Customized Flagelliform Spidroins Form Spider Silk-like Fibers at pH 8.0 with Outstanding Tensile Strength.ACS biomaterials science & engineering · 2022Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Spider aciniform (or wrapping) silk is the toughest of the seven types of spider silks/glue due to a combination of high elasticity and strength. Like most spider silk proteins (spidroins), aciniform spidroin (AcSp1) has a large core repetitive domain flanked by relatively short N- and C-terminal nonrepetitive domains (the NTD and CTD, respectively). The major ampullate silk protein (MaSp) CTD has been shown to control protein solubility and fiber formation, but the aciniform CTD function remains unknown. Here, we compare fiber mechanical properties, solution-state structuring, and fibrous state secondary structural composition, and orientation relative to native aciniform silk for two AcSp1 repeat units with or without fused AcSp1- and MaSp-derived CTDs alongside three AcSp1 repeat units without a CTD. The native AcSp1 CTD uniquely modulated fiber mechanical properties, relative to all other constructs, directly correlating to a native-like structural transformation and alignment.
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Registered trials
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.