Liu Y.Wu H.-C.Bhokisham N.Li J.Hong K.-L.Quan D.N.Tsao C.-Y.Bentley W.E.Payne G.F.HSUAN-CHEN WU2020-02-132020-02-13201810431802https://scholars.lib.ntu.edu.tw/handle/123456789/458336https://www.scopus.com/inward/record.uri?eid=2-s2.0-85046946129&doi=10.1021%2facs.bioconjchem.8b00197&partnerID=40&md5=29a0763f4c7e6acbd745a3d71bad0a46Biology often provides the inspiration for functional soft matter, but biology can do more: it can provide the raw materials and mechanisms for hierarchical assembly. Biology uses polymers to perform various functions, and biologically derived polymers can serve as sustainable, self-assembling, and high-performance materials platforms for life-science applications. Biology employs enzymes for site-specific reactions that are used to both disassemble and assemble biopolymers both to and from component parts. By exploiting protein engineering methodologies, proteins can be modified to make them more susceptible to biology's native enzymatic activities. They can be engineered with fusion tags that provide (short sequences of amino acids at the C- and/or N- termini) that provide the accessible residues for the assembling enzymes to recognize and react with. This "biobased" fabrication not only allows biology's nanoscale components (i.e., proteins) to be engineered, but also provides the means to organize these components into the hierarchical structures that are prevalent in life. © 2018 American Chemical Society.[SDGs]SDG3Biochemical engineering; Enzymes; Genetic engineering; Component part; Hierarchical assemblies; High performance material; Life-sciences; Protein engineering; Science applications; Self-assembling; Site-specific; Soft matter; Various functions; Biology; nucleophile; peroxidase; polymer; protein glutamine gamma glutamyltransferase; amino acid; bacterial protein; biomaterial; monophenol monooxygenase; protein; protein glutamine gamma glutamyltransferase; amino acid sequence; catalyst; cell function; controlled study; covalent bond; enzyme activity; enzyme mechanism; human; molecular weight; nanofabrication; nucleophilicity; protein assembly; protein cross linking; protein engineering; protein hydrolysis; Review; temperature; thermostability; animal; bacterium; biocatalysis; bioengineering; chemistry; genetics; metabolism; molecular model; procedures; protein engineering; quorum sensing; Amino Acids; Animals; Bacteria; Bacterial Proteins; Biocatalysis; Biocompatible Materials; Bioengineering; Humans; Models, Molecular; Monophenol Monooxygenase; Protein Engineering; Proteins; Quorum Sensing; Transglutaminasesreview10.1021/acs.bioconjchem.8b00197297456512-s2.0-85046946129https://www2.scopus.com/inward/record.uri?eid=2-s2.0-85046946129&doi=10.1021%2facs.bioconjchem.8b00197&partnerID=40&md5=29a0763f4c7e6acbd745a3d71bad0a46