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*

*Tämän työn vastaava kirjoittaja

Tutkimustuotos: LehtiartikkeliArticleScientificvertaisarvioitu

19 Lataukset (Pure)

Abstrakti

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.

AlkuperäiskieliEnglanti
Sivut3142-3153
Sivumäärä12
JulkaisuBiomacromolecules
Vuosikerta23
Numero8
Varhainen verkossa julkaisun päivämäärä7 heinäk. 2022
DOI - pysyväislinkit
TilaJulkaistu - 8 elok. 2022
OKM-julkaisutyyppiA1 Julkaistu artikkeli, soviteltu

Sormenjälki

Sukella tutkimusaiheisiin 'Liquid-Liquid Phase Separation and Assembly of Silk-like Proteins is Dependent on the Polymer Length'. Ne muodostavat yhdessä ainutlaatuisen sormenjäljen.

Siteeraa tätä