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More than one way to spin a crystallite: multiple trajectories through liquid crystallinity to solid silk
Andrew A Walker1, Chris Holland2, Tara D Sutherland3
1Research School of Biology, Australian National University, Canberra 0200, Australia Food and Nutrition, CSIRO, Canberra 2600, Australia a.walker@uq.edu.au.
Proceedings. Biological Sciences
|June 5, 2015
Summary
This review compares canonical and non-canonical silk proteins, highlighting differences in structure and processing. Understanding these variations, particularly in liquid crystal mesogens, can advance biomaterial development.
Area of Science:
- Biomaterials Science
- Protein Engineering
- Structural Biology
Background:
- Arthropods process protein solutions (silk dope) into solid silk fibers, facing challenges with viscosity and structure formation.
- Convergent evolution shows silk-producing organisms utilize liquid crystal intermediates (mesophases) for efficient silk processing.
- The precise nature of silk dope mesogens and their link to liquid crystallinity, protein structure, and fiber formation requires further investigation.
Purpose of the Study:
- To compare the differences in liquid crystal mesogens and processing between canonical silks (silkworms, spiders) and non-canonical silks (other insects).
- To analyze amino acid sequences and processing of natural, regenerated, and recombinant silk proteins.
- To explore the potential of non-canonical silk proteins for advanced biomaterial development.
Main Methods:
- Comparative analysis of amino acid sequences and protein structures.
- Review of natural, regenerated, and recombinant silk protein processing.
- Examination of liquid crystallinity and mesophase formation in different silk types.
Main Results:
- Canonical silk proteins are long, flexible, and amphipathic, forming micelle-like mesogens that transition to crystallites upon deformation.
- Non-canonical silk proteins are short with rod-like structures, serving as both mesogens and crystallites without significant phase transition.
- Significant differences exist in length, architecture, amino acid content, and folding between canonical and non-canonical silk proteins.
Conclusions:
- Non-canonical silk proteins offer a promising avenue for biomaterial development due to their inherent structure and high production yields.
- Elucidating the processing of non-canonical silk proteins can lead to novel strategies for creating advanced protein-based materials.
- The distinct structural and processing mechanisms of canonical versus non-canonical silks provide valuable insights for biomaterial design.
