Genetic engineering of fibrous proteins: spider dragline silk and collagen

Adv Drug Deliv Rev. 2002 Oct 18;54(8):1131-43. doi: 10.1016/s0169-409x(02)00061-3.


Various strategies have been employed to genetically engineer fibrous proteins. Two examples, the subject of this review, include spider dragline silk from Nephila clavipes and collagen. These proteins are highlighted because of their unique mechanical and biological properties related to controlled release, biomaterials and tissue engineering. Cloning and expression of native genes and synthetic artificial variants of the consensus sequence repeats from the native genes has been accomplished. Expression of recombinant silk and collagen proteins has been reported in a variety of host systems, including bacteria, yeast, insect cells, plants and mammalian cells. Future utility for these proteins for biomedical materials is expected to increase as needs expand for designer materials with tailored mechanical properties and biological interactions to elicit specific responses in vitro and in vivo.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Collagen / chemical synthesis*
  • Collagen / genetics*
  • Fibroins*
  • Genes, Synthetic
  • Humans
  • Molecular Sequence Data
  • Protein Engineering / methods*
  • Proteins / chemical synthesis*
  • Proteins / genetics*
  • Spiders


  • Proteins
  • spidroin 2
  • Collagen
  • Fibroins