Tailoring the formation and stability of self-assembled structures from precisely engineered intrinsically disordered protein polymers: A comprehensive review

Doole, Fathima T.; Camp, Christopher P.; Kim, Minkyu

doi:10.1016/j.giant.2023.100158

Cited by 1 publication

(1 citation statement)

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“…In addition to the precise control over their composition, molecular weight, and monodispersity, noncanonical amino acids can be installed to further expand their chemical functionality. [66,67] While other stimuli such as pH, ionic strength, enzymes, redox, magnetic field can also be used to alter conformational properties of polypeptides, [68] this review focuses on recent reports [4,7,[69][70][71][72] harnessing the thermally triggered assembly behavior of such genetically fused hybrid constructs.…”

Section: Introductionmentioning

confidence: 99%

Genetically Fusing Order‐Promoting and Thermoresponsive Building Blocks to Design Hybrid Biomaterials

Patkar,

Wang,

Mosquera

et al. 2024

Chemistry A European J

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The unique biophysical and biochemical properties of intrinsically disordered proteins (IDPs) and their recombinant derivatives, intrinsically disordered protein polymers (IDPPs) offer opportunities for producing multistimuli‐responsive materials; their sequence‐encoded disorder and tendency for phase separation facilitate the development of multifunctional materials. This review highlights the strategies for enhancing the structural diversity of elastin‐like polypeptides (ELPs) and resilin‐like polypeptides (RLPs), and their self‐assembled structures via genetic fusion to ordered motifs such as helical or beta sheet domains. In particular, this review describes approaches that harness the synergistic interplay between order‐promoting and thermoresponsive building blocks to design hybrid biomaterials, resulting in well‐structured, stimuli‐responsive supramolecular materials ordered on the nanoscale.

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