ArticleBiomacromolecules2022
Liquid-Liquid Phase Separation and Assembly of Silk-like Proteins is Dependent on the Polymer Length.
Article in Biomacromolecules, 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.
- Induced Proximity Approach Enables the Recombinant Production of Polyphosphorylated Silk Proteins with Improved Adhesiveness.Biomacromolecules · 2025Article
- Probing the Interplay of Protein Self-Assembly and Covalent Bond Formation in Photo-Crosslinked Silk Fibroin Hydrogels.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Progress in Multiscale Modeling of Silk Materials.Biomacromolecules · 2024Review
- Spidroins under the Influence of Alcohol: Effect of Ethanol on Secondary Structure and Molecular Level Solvation of Silk-Like Proteins.Biomacromolecules · 2023Article
- Display of multiple proteins on engineered canine parvovirus-like particles expressed in cultured silkworm cells and silkworm larvae.Frontiers in bioengineering and biotechnology · 2023Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phase transitions have an essential role in the assembly of nature's protein-based materials into hierarchically organized structures, yet many of the underlying mechanisms and interactions remain to be resolved. A central question for designing proteins for materials is how the protein architecture and sequence affects the nature of the phase transitions and resulting assembly. In this work, we produced 82 kDa (1×), 143 kDa (2×), and 204 kDa (3×) silk-mimicking proteins by taking advantage of protein ligation by SpyCatcher/Tag protein-peptide pair. We show that the three silk proteins all undergo a phase transition from homogeneous solution to assembly formation. In the assembly phase, a length- and concentration-dependent transition between two distinct assembly morphologies, one forming aggregates and another coacervates, exists. The coacervates showed properties that were dependent on the protein size. Computational modeling of the proteins by a bead-spring model supports the experimental results and provides us a possible mechanistic origin for the assembly transitions based on architectures and interactions.
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Registered trials
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