title: Biomimetic spinning of artificial spider silk from a chimeric minispidroin.
abstract: Herein we present a chimeric recombinant spider silk protein (spidroin) whose aqueous solubility equals that of native spider silk dope and a spinning device that is based solely on aqueous buffers, shear forces and lowered pH. The process recapitulates the complex molecular mechanisms that dictate native spider silk spinning and is highly efficient; spidroin from one liter of bacterial shake-flask culture is enough to spin a kilometer of the hitherto toughest as-spun artificial spider silk fiber.
authors.affiliation: Department of Anatomy, Physiology and Biochemistry, Swedish University of Agricultural Sciences, Uppsala, Sweden.
authors.forename: Marlene
authors.initials: M
authors.lastname: Andersson
authors.affiliation: Institute of Biological Sciences and Biotechnology, Donghua University, Shanghai, P.R. China.
authors.forename: Qiupin
authors.initials: Q
authors.lastname: Jia
authors.affiliation: ETSI de Caminos and Center for Biomedical Technology, Universidad Politécnica de Madrid, Madrid, Spain.
authors.forename: Ana
authors.initials: A
authors.lastname: Abella
authors.affiliation: ETSI de Caminos and Center for Biomedical Technology, Universidad Politécnica de Madrid, Madrid, Spain.
authors.forename: Xiau-Yeen
authors.initials: XY
authors.lastname: Lee
authors.affiliation: Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, UK.
authors.forename: Michael
authors.initials: M
authors.lastname: Landreh
authors.affiliation: Department of Biosciences and Nutrition, Karolinska Institutet, Stockholm, Sweden.|School of Technology and Health, KTH Royal Institute of Technology, Stockholm, Sweden.
authors.forename: Pasi
authors.initials: P
authors.lastname: Purhonen
authors.affiliation: Department of Biosciences and Nutrition, Karolinska Institutet, Stockholm, Sweden.|School of Technology and Health, KTH Royal Institute of Technology, Stockholm, Sweden.
authors.forename: Hans
authors.initials: H
authors.lastname: Hebert
authors.affiliation: Department of Engineering Sciences, SciLifeLab, Uppsala University, Uppsala, Sweden.|Department of Biomedical Engineering, Lund University, Lund, Sweden.
authors.forename: Maria
authors.identifier: 0000-0002-1264-1337
authors.initials: M
authors.lastname: Tenje
authors.affiliation: Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, UK.
authors.forename: Carol V
authors.initials: CV
authors.lastname: Robinson
authors.affiliation: Institute of Biological Sciences and Biotechnology, Donghua University, Shanghai, P.R. China.
authors.forename: Qing
authors.initials: Q
authors.lastname: Meng
authors.affiliation: ETSI de Caminos and Center for Biomedical Technology, Universidad Politécnica de Madrid, Madrid, Spain.
authors.forename: Gustavo R
authors.initials: GR
authors.lastname: Plaza
authors.affiliation: Department of Anatomy, Physiology and Biochemistry, Swedish University of Agricultural Sciences, Uppsala, Sweden.|Department of Neurobiology, Care Sciences and Society (NVS), Karolinska Institutet, Stockholm, Sweden.
authors.forename: Jan
authors.initials: J
authors.lastname: Johansson
authors.affiliation: Department of Anatomy, Physiology and Biochemistry, Swedish University of Agricultural Sciences, Uppsala, Sweden.|Department of Neurobiology, Care Sciences and Society (NVS), Karolinska Institutet, Stockholm, Sweden.
authors.forename: Anna
authors.identifier: 0000-0002-1872-1207
authors.initials: A
authors.lastname: Rising
mesh_terms: D000818:Animals; D032701:Biomimetics; D005349:Fibroins / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D011994:Recombinant Proteins / Q000737:chemistry
chemical_list: D011994:Recombinant Proteins; D005349:Fibroins