A Novel Model System for Design of Biomaterials Based on Recombinant Analogs of Spider Silk Proteins

  • Vladimir G. Bogush
  • Olga S. Sokolova
  • Lyubov I. Davydova
  • Dmitri V. Klinov
  • Konstantin V. Sidoruk
  • Natalya G. Esipova
  • Tatyana V. Neretina
  • Igor A. Orchanskyi
  • Vsevolod Yu Makeev
  • Vladimir G. Tumanyan
  • Konstantin V. Shaitan
  • Vladimir G. Debabov
  • Mikhail P. Kirpichnikov
Original Article

DOI: 10.1007/s11481-008-9129-z

Cite this article as:
Bogush, V.G., Sokolova, O.S., Davydova, L.I. et al. J Neuroimmune Pharmacol (2009) 4: 17. doi:10.1007/s11481-008-9129-z

Abstract

Spider dragline silk possesses impressive mechanical and biochemical properties. It is synthesized by a couple of major ampullate glands in spiders and comprises of two major structural proteins—spidroins 1 and 2. The relationship between structure and mechanical properties of spider silk is not well understood. Here, we modeled the complete process of the spider silk assembly using two new recombinant analogs of spidroins 1 and 2. The artificial genes sequence of the hydrophobic core regions of spidroin 1 and 2 have been designed using computer analysis of existing databases and mathematical modeling. Both proteins were expressed in Pichia pastoris and purified using a cation exchange chromatography. Despite the absence of hydrophilic N- and C-termini, both purified proteins spontaneously formed the nanofibrils and round micelles of about 1 μm in aqueous solutions. The electron microscopy study has revealed the helical structure of a nanofibril with a repeating motif of 40 nm. Using the electrospinning, the thin films with an antiparallel β-sheet structure were produced. In summary, we were able to obtain artificial structures with characteristics that are perspective for further biomedical applications, such as producing three-dimensional matrices for tissue engineering and drug delivery.

Keywords

spidroin 1 and 2 nanofibrils electrospinning antiparallel β-sheet structure atomic force microscopy scanning electron microscopy 

Abbreviations

PPII

poly-l-proline

FTIR

Fourier transform infrared spectroscopy

Copyright information

© Springer Science+Business Media, LLC 2008

Authors and Affiliations

  • Vladimir G. Bogush
    • 1
  • Olga S. Sokolova
    • 2
    • 3
  • Lyubov I. Davydova
    • 1
  • Dmitri V. Klinov
    • 4
  • Konstantin V. Sidoruk
    • 1
  • Natalya G. Esipova
    • 5
  • Tatyana V. Neretina
    • 4
  • Igor A. Orchanskyi
    • 2
  • Vsevolod Yu Makeev
    • 1
  • Vladimir G. Tumanyan
    • 5
  • Konstantin V. Shaitan
    • 2
  • Vladimir G. Debabov
    • 1
  • Mikhail P. Kirpichnikov
    • 2
  1. 1.State Scientific Center “GosNIIGenetika”MoscowRussia
  2. 2.Faculty of Biology, Department of BioengineeringMoscow State UniversityMoscowRussia
  3. 3.Institute of BiochemistryRASMoscowRussia
  4. 4.Institute of Bioorganic ChemistryRASMoscowRussia
  5. 5.Engelhardt Institute of Molecular BiologyRASMoscowRussia