title: Effect of sequence features on assembly of spider silk block copolymers.
abstract: Bioengineered spider silk block copolymers were studied to understand the effect of protein chain length and sequence chemistry on the formation of secondary structure and materials assembly. Using a combination of in vitro protein design and assembly studies, we demonstrate that silk block copolymers possessing multiple repetitive units self-assemble into lamellar microstructures. Additionally, the study provides insights into the assembly behavior of spider silk block copolymers in concentrated salt solutions.
authors.affiliation: Department of Biomedical Engineering, Tufts University, Medford, MA 02155, USA.
authors.forename: Olena S
authors.initials: OS
authors.lastname: Tokareva
authors.affiliation: Department of Civil and Environmental Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
authors.forename: Shangchao
authors.initials: S
authors.lastname: Lin
authors.affiliation: Department of Biomedical Engineering, Division of Materials Science and Engineering, Boston University, Boston, MA 02215, USA.
authors.forename: Matthew M
authors.initials: MM
authors.lastname: Jacobsen
authors.affiliation: Department of Biomedical Engineering, Tufts University, Medford, MA 02155, USA; Department of Physics and Astronomy, Center for Nanoscopic Physics, Tufts University, Medford, MA 02155, USA.
authors.forename: Wenwen
authors.initials: W
authors.lastname: Huang
authors.affiliation: Department of Physics and Astronomy, Center for Nanoscopic Physics, Tufts University, Medford, MA 02155, USA.
authors.forename: Daniel
authors.initials: D
authors.lastname: Rizzo
authors.affiliation: Department of Biomedical Engineering, Division of Materials Science and Engineering, Boston University, Boston, MA 02215, USA.
authors.forename: David
authors.initials: D
authors.lastname: Li
authors.affiliation: Department of Physics and Astronomy, Center for Nanoscopic Physics, Tufts University, Medford, MA 02155, USA.
authors.forename: Marc
authors.initials: M
authors.lastname: Simon
authors.affiliation: Department of Physics and Astronomy, Center for Nanoscopic Physics, Tufts University, Medford, MA 02155, USA.
authors.forename: Cristian
authors.initials: C
authors.lastname: Staii
authors.affiliation: Department of Physics and Astronomy, Center for Nanoscopic Physics, Tufts University, Medford, MA 02155, USA.
authors.forename: Peggy
authors.initials: P
authors.lastname: Cebe
authors.affiliation: Department of Biomedical Engineering, Division of Materials Science and Engineering, Boston University, Boston, MA 02215, USA.
authors.forename: Joyce Y
authors.initials: JY
authors.lastname: Wong
authors.affiliation: Department of Civil and Environmental Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
authors.forename: Markus J
authors.initials: MJ
authors.lastname: Buehler
authors.affiliation: Department of Biomedical Engineering, Tufts University, Medford, MA 02155, USA. Electronic address: David.Kaplan@tufts.edu.
authors.forename: David L
authors.initials: DL
authors.lastname: Kaplan
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D006639:Histidine / Q000737:chemistry; D057927:Hydrophobic and Hydrophilic Interactions; D008027:Light; D018625:Microscopy, Atomic Force; D008855:Microscopy, Electron, Scanning; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015202:Protein Engineering / Q000379:methods; D011994:Recombinant Proteins / Q000737:chemistry*; D020449:Repetitive Sequences, Amino Acid; D012542:Scattering, Radiation; D047011:Silk / Q000737:chemistry* / Q000378:metabolism; D017550:Spectroscopy, Fourier Transform Infrared; D013112:Spiders / Q000737:chemistry*; D013329:Structure-Activity Relationship
chemical_list: D011994:Recombinant Proteins; D047011:Silk; D006639:Histidine
keywords: Block copolymers; Modeling; Self-assembly; Silk