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

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 f...

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Bibliographic Details
Published in:Applied physics. A, Materials science & processing Materials science & processing, 2006-02, Vol.82 (2), p.223-233
Main Authors: Foo, C. Wong Po, Bini, E., Hensman, J., Knight, D.P., Lewis, R.V., Kaplan, D.L.
Format: Article
Language:English
Subjects:
Applied physics
Assembly
Calcium ions
Ducts
Hydrogen bonding
Hydrophobicity
Insects
Materials science
Mechanical properties
Moisture content
NMR
Nuclear magnetic resonance
Proteins
Raman spectroscopy
Silk
Silkworms
Spiders
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Summary: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.
ISSN:0947-8396
1432-0630
DOI:10.1007/s00339-005-3426-7