title: Nanoparticle self-assembly by a highly stable recombinant spider wrapping silk protein subunit.
abstract: Artificial spider silk proteins may form fibers with exceptional strength and elasticity. Wrapping silk, or aciniform silk, is the toughest of the spider silks, and has a very different protein composition than other spider silks. Here, we present the characterization of an aciniform protein (AcSp1) subunit named W1, consisting of one AcSp1 199 residue repeat unit from Argiope trifasciata. The structural integrity of recombinant W1 is demonstrated in a variety of buffer conditions and time points. Furthermore, we show that W1 has a high thermal stability with reversible denaturation at ∼71°C and forms self-assembled nanoparticle in near-physiological conditions. W1 therefore represents a highly stable and structurally robust module for protein-based nanoparticle formation.
authors.affiliation: Institute of Biological Sciences and Biotechnology, Donghua University, Shanghai 201620, PR China; Department of Biochemistry & Molecular Biology, Dalhousie University, Halifax, NS B3H 4R2, Canada.
authors.forename: Lingling
authors.initials: L
authors.lastname: Xu
authors.forename: Marie-Laurence
authors.initials: ML
authors.lastname: Tremblay
authors.forename: Kathleen E
authors.initials: KE
authors.lastname: Orrell
authors.forename: Jérémie
authors.initials: J
authors.lastname: Leclerc
authors.forename: Qing
authors.initials: Q
authors.lastname: Meng
authors.forename: Xiang-Qin
authors.initials: XQ
authors.lastname: Liu
authors.forename: Jan K
authors.initials: JK
authors.lastname: Rainey
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D008969:Molecular Sequence Data; D053758:Nanoparticles; D011994:Recombinant Proteins / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid; D047011:Silk / Q000737:chemistry*; D013112:Spiders / Q000737:chemistry*
chemical_list: D011994:Recombinant Proteins; D047011:Silk
keywords: 8-anilino-1-naphthalenesulfonic acid; ANS; AcSp1; Argiope trifasciata AcSp1; Argiope trifasciata aciniform spidroin 1; Biomaterial; CD; DLS; EM; NMR; Nanoparticle; SEM; Spider silk protein; T(m); TEM; UV; W(1); circular dichroism; dynamic light scattering; electron microscopy; nuclear magnetic resonance; scanning electron microscopy; subunit of the repetitive domain of AcSp1; thermal denaturation midpoint; transmission electron microscopy; ultraviolet; wavelength of maximum of emission intensity; wavelengths of emission and excitation, respectively; λ(em) and λ(ex); λ(max)