title: Natural templates for coiled-coil biomaterials from praying mantis egg cases.
abstract: Whereas there is growing interest in producing biomaterials containing coiled-coils, relatively few studies have made use of naturally occurring fibrous proteins. In this study, we have characterized fibrous proteins used by mother praying mantises to produce an extensive covering for their eggs called an ootheca and demonstrate the production of artificial ootheca using recombinantly produced proteins. Examination of natural oothecae by infrared spectroscopy and solid-state nuclear magnetic resonance revealed the material to consist of proteins organized predominately as coiled-coils. Two structural proteins, Mantis Fibroin 1 and Mantis Fibroin 2, were identified in ootheca from each of three species. Between species, the primary sequences of both proteins had diverged considerably, but other features were tightly conserved, including low molecular weight, high abundance of Ala, Glu, Lys, and Ser, and a triblock-like architecture with extensive central coiled-coil domain. Mantis fibroin hydrophobic cores had an unusual composition containing high levels of alanine and aromatic residues. Recombinantly produced mantis fibroins folded into coiled-coils in solution and could be fabricated into solid materials with high coiled-coil content. The structural features of mantis fibroins and their straightforward recombinant production make them promising templates for the production of coiled-coil biomimetics materials.
authors.affiliation: Research School of Biology, Australian National University, Canberra, Australia, 0200.
authors.forename: Andrew A
authors.initials: AA
authors.lastname: Walker
authors.forename: Sarah
authors.initials: S
authors.lastname: Weisman
authors.forename: Tsunenori
authors.initials: T
authors.lastname: Kameda
authors.forename: Tara D
authors.initials: TD
authors.lastname: Sutherland
mesh_terms: D000409:Alanine / Q000737:chemistry; D000595:Amino Acid Sequence; D000818:Animals; D001672:Biocompatible Materials / Q000737:chemistry*; D040761:Biomimetic Materials / Q000138:chemical synthesis*; D002942:Circular Dichroism; D004926:Escherichia coli / Q000235:genetics; D005260:Female; D005349:Fibroins / Q000737:chemistry* / Q000235:genetics; D015723:Gene Library; D018698:Glutamic Acid / Q000737:chemistry; D057927:Hydrophobic and Hydrophilic Interactions; D008239:Lysine / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D020050:Mantodea / Q000737:chemistry*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010063:Ovum; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D012596:Scleroproteins / Q000737:chemistry; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D012694:Serine / Q000737:chemistry
chemical_list: D001672:Biocompatible Materials; D011994:Recombinant Proteins; D012596:Scleroproteins; D018698:Glutamic Acid; D012694:Serine; D005349:Fibroins; D008239:Lysine; D000409:Alanine