Unnatural amino acids program thermoresponsive protein-polymer diblocks into shape-shifting nanostructures.

Authors

Daniela S Strugach, Yuval Pasternak, Oren Tiv, Federico Kaufman, Itzhak Levi, Miriam Amiram

Published in

Trends in biotechnology. Sep 29, 2026. Epub Sep 29, 2026.

Abstract

Control over the morphology and function of self-assembling polymers remains a central challenge in engineering adaptive biomaterials and synthetic biological systems. Here, we establish that recombinant elastin-like polypeptide-resilin-like polypeptide diblocks can be programmed through incorporation of unnatural amino acids (uAAs) to undergo multistep, temperature-dependent phase transitions that generate shape-shifting nanostructures, including micelles, vesicles, and higher-order assemblies not typically accessible in conventional protein materials, thereby expanding their structural and functional design space. Incorporation of only six uAAs (<1.5% of residues) is sufficient to program phase behavior and assembly pathways, with uAA hydrophobicity and sequence position governing morphology and structural transitions. Photo-switchable uAAs further enable reversible, light-driven control over nanostructure morphology, modulating substrate encapsulation and enzymatic activity. Together, these findings define a genetically encoded design framework for adaptive protein materials and expand opportunities for their use in biotechnology, including synthetic organelle-like systems, dynamic biomolecular assemblies, responsive biocatalysis, and drug delivery.

PMID:
42810892
Bibliographic data and abstract were imported from PubMed on 30 Sep 2026.

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