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Cutting Edge Structural Protein from the Jaws of Nereis virens

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Chris C. Broomell*^†, Sue F. Chase^‡, Tom Laue^‡ and J. Herbert Waite^†

University of California at Santa Barbara, Santa Barbara, California 93106, and Center to Advance Molecular Interaction Science, University of New Hampshire, Durham, New Hampshire 03824

Biomacromolecules, 2008, 9 (6), pp 1669–1677

DOI: 10.1021/bm800200a

Publication Date (Web): May 23, 2008

* To whom correspondence should be addressed. Email: broomell@lifesci.ucsb.edu., †

UC at Santa Barbara.

, ‡

University of New Hampshire.

Abstract

The fang-like jaws of the marine polychaete Nereis virens possess remarkable mechanical properties considering their high protein content and lack of mineralization. Hardness and stiffness properties in the jaw tip are comparable to human dentin and are achieved by extensive coordination of Zn²⁺ by a histidine-rich protein framework. In the present study, the predominant protein in the jaw tip, Nvjp-1, was purified and characterized by partial peptide mapping and molecular cloning of a partial cDNA from a jaw pulp library. The deduced amino acid sequence revealed an 38 kDa histidine-rich protein rich in glycine and histidine (36 and 27%, respectively) with no well-defined repetitive motifs. The effects of pH and metal treatment on aggregation, secondary structure, and hydrodynamic properties of recombinant Nvjp-1 are described. Notably, Zn treatment induced the formation of amyloid-like fibers.

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This article has been cited by 1 ACS Journal articles (1 most recent appear below).

Ragworm Jaw-Inspired Metal Ion Cross-Linking for Improved Mechanical Properties of Polymer Blends
Aasheesh Srivastava, Niels Holten-Andersen, Galen D. Stucky and J. Herbert Waite
Biomacromolecules2008 9 (10), 2873-2880
- Ragworm Jaw-Inspired Metal Ion Cross-Linking for Improved Mechanical Properties of Polymer Blends
  Aasheesh Srivastava, Niels Holten-Andersen, Galen D. Stucky and J. Herbert Waite
  Biomacromolecules2008 9 (10), 2873-2880
  Several naturally occurring biomacromolecular structures, particularly those containing histidine-rich proteins, have been shown to depend on metal ion complexation for hardness and stiffness. In this study, water-soluble metal-binding polymers and ...
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