Liquid-Liquid Phase Separation and Assembly of Silk-like Proteins is Dependent on the Polymer Length

Laura Lemetti, Alberto Scacchi, Yin Yin, Mengjie Shen, Markus B. Linder, Maria Sammalkorpi*, A. Sesilja Aranko*

*Corresponding author for this work

Research output: Contribution to journalArticleScientificpeer-review

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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.

Original languageEnglish
Pages (from-to)3142-3153
Number of pages12
JournalBiomacromolecules
Volume23
Issue number8
Early online date7 Jul 2022
DOIs
Publication statusPublished - 8 Aug 2022
MoE publication typeA1 Journal article-refereed

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