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Spider silk protein refolding is controlled by changing pH.

Cedric Dicko1, Fritz Vollrath, John M Kenney

  • 1Department of Zoology, Oxford University, OX1 3PS Oxford, United Kingdom. cedric.dicko@zoology.oxac.uk

Biomacromolecules
|May 11, 2004
PubMed
Summary

Spider silk proteins called spidroins undergo structural changes due to a decreasing pH within the silk gland. This pH drop is crucial for transforming spidroins into the beta-sheet structures essential for strong dragline silk formation.

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Area of Science:

  • Biomaterials Science
  • Protein Chemistry
  • Structural Biology

Background:

  • Spidroins are the primary proteins in spider dragline silk.
  • These proteins originate from two distinct tissue layers (A and B) in the major ampullate gland.
  • Silk thread formation occurs in the gland's duct lumen.

Purpose of the Study:

  • To investigate the pH changes within the spider silk gland during spidroin processing.
  • To correlate these pH changes with the structural folding of spidroins.
  • To elucidate the role of pH in spider silk formation.

Main Methods:

  • Utilized pH-sensitive microelectrode probes to measure pH gradients.
  • Employed circular dichroism spectroscopy to analyze protein structural changes.

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  • Conducted in vitro experiments to assess pH-induced conformational changes.
  • Performed amino acid analyses to identify distinct spidroins.

    • Main Results:

    • A monotonic decrease in pH from 7.2 to 6.3 was observed along the gland and duct.
    • Structural refolding of spidroins was detected, correlating with gland position and pH.
    • Lowering pH in vitro induced an irreversible conformational change from coil to beta-sheet structure in A-zone proteins.
    • Distinct spidroins secreted from A and B zones suggest a role in acidification and folding sensitivity.

    Conclusions:

    • A quantitative map of pH and spidroin folding within the silk gland was established.
    • pH is a critical factor in the structural transformation of spidroins.
    • The findings provide new insights into the mechanism of spider silk formation.