Effect of sequence features on assembly of spider silk block copolymers

Olena S Tokareva; Shangchao Lin; Matthew M Jacobsen; Wenwen Huang; Daniel Rizzo; David Li; Marc Simon; Cristian Staii; Peggy Cebe; Joyce Y Wong; Markus J Buehler; David L Kaplan

doi:10.1016/j.jsb.2014.03.004

Effect of sequence features on assembly of spider silk block copolymers

J Struct Biol. 2014 Jun;186(3):412-9. doi: 10.1016/j.jsb.2014.03.004. Epub 2014 Mar 12.

Authors

Affiliations

¹ Department of Biomedical Engineering, Tufts University, Medford, MA 02155, USA.
² Department of Civil and Environmental Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
³ Department of Biomedical Engineering, Division of Materials Science and Engineering, Boston University, Boston, MA 02215, USA.
⁴ 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.
⁵ Department of Physics and Astronomy, Center for Nanoscopic Physics, Tufts University, Medford, MA 02155, USA.
⁶ Department of Biomedical Engineering, Tufts University, Medford, MA 02155, USA. Electronic address: David.Kaplan@tufts.edu.

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.

Keywords: Block copolymers; Modeling; Self-assembly; Silk.

Publication types

Research Support, N.I.H., Extramural

MeSH terms

Amino Acid Sequence
Animals
Histidine / chemistry
Hydrophobic and Hydrophilic Interactions
Light
Microscopy, Atomic Force
Microscopy, Electron, Scanning
Models, Molecular
Molecular Sequence Data
Protein Engineering / methods
Recombinant Proteins / chemistry*
Repetitive Sequences, Amino Acid
Scattering, Radiation
Silk / chemistry*
Silk / metabolism
Spectroscopy, Fourier Transform Infrared
Spiders / chemistry*
Structure-Activity Relationship

Substances

Recombinant Proteins
Silk
Histidine

Grants and funding

U01 EB014976/EB/NIBIB NIH HHS/United States