Applied Physics A

, Volume 82, Issue 2, pp 223–233 | Cite as

Role of pH and charge on silk protein assembly in insects and spiders

  • C. Wong Po Foo
  • E. Bini
  • J. Hensman
  • D.P. Knight
  • R.V. Lewis
  • D.L. Kaplan
Article

Abstract

Silk fibers possess impressive mechanical properties, dependant, in part, on the crystalline β-sheets silk II conformation. The transition to silk II from soluble silk I-like conformation in silk glands, is thought to originate in the spinning ducts immediately before the silk is drawn down into a fiber. However the assembly process of these silk molecules into fibers, whether in silkworms or spiders, is not well understood. Extensional flow, protein concentration, pH and metal ion concentrations are thought to be most important in in vivo silk processing and in affecting structural conformations. We look at how parameters such as pH, [Ca2+], [K+], and [Cu2+], and water content, interact with the domain structure of silk proteins towards the successful storage and processing of these concentrated hydrophobic silk proteins. Our recent domain mapping studies of all known silk proteins, and 2D Raman spectroscopy, NMR, and DLS studies performed on sections of silkworm gland, suggest that low pH and gradual water removal promote intermolecular over intramolecular hydrogen bonding. This discussion helps to provide the necessary ground rules towards the design of silk protein analogues with specific hydrophobicity and charge profiles to optimize expression, solubility and assembly with implications in structural biology and material science.

Keywords

Silk Gland Silk Protein Spider Silk Posterior Division Anterior Division 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag 2005

Authors and Affiliations

  • C. Wong Po Foo
    • 1
    • 2
  • E. Bini
    • 3
  • J. Hensman
    • 4
  • D.P. Knight
    • 4
  • R.V. Lewis
    • 5
  • D.L. Kaplan
    • 1
  1. 1.Department of Biomedical Engineering & Bioengineering CenterTufts UniversityMedfordUSA
  2. 2.Department of ChemistryTufts UniversityMedfordUSA
  3. 3.Department of Biochemistry and MicrobiologyRutgers UniversityNew BrunswickUSA
  4. 4.Department of ZoologyOxford UniversityOxfordUK
  5. 5.Department of Molecular BiologyUniversity of WyomingLaramieUSA

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