| Literature DB >> 28337848 |
Sydney Hollingshead1, Charng-Yu Lin1, Julie C Liu1,2.
Abstract
Recombinant protein design allows modular protein domains with different functionalities and responsive behaviors to be easily combined. Inclusion of these protein domains can enable recombinant proteins to have complex responses to their environment (e.g., temperature-triggered aggregation followed by enzyme-mediated cleavage for drug delivery or pH-triggered conformational change and self-assembly leading to structural stabilization by adjacent complementary residues). These "smart" behaviors can be tuned by amino acid identity and sequence, chemical modifications, and addition of other components. A wide variety of domains and peptides have smart behavior. This review focuses on protein designs for self-assembly or conformational changes due to stimuli such as shifts in temperature or pH.Entities:
Keywords: biomaterials; biopolymers; hydrogels; self-assembly; stimuli-sensitive polymers
Mesh:
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Year: 2017 PMID: 28337848 PMCID: PMC6020822 DOI: 10.1002/mabi.201600554
Source DB: PubMed Journal: Macromol Biosci ISSN: 1616-5187 Impact factor: 4.979