Lipid-specific β-sheet formation in a mussel byssus protein domain

Biomacromolecules. 2013 Sep 9;14(9):3238-45. doi: 10.1021/bm400860y. Epub 2013 Aug 29.


Intrinsically disordered proteins (IDP) or regions (IDR) can adopt multiple conformational states, depending on the interaction partners they encounter. This enables proteins or individual domains to fulfill multiple functions. Here, we analyzed the flank sequences of preCol-NG, one of three collagenous proteins of a mussel byssus thread governing its mechanical performance. preCol-NG comprises a collagen domain and nonrepetitive termini enclosing specific flank regions characterized by tandem repeats known from silk proteins, protein elastomers, and plant cell wall-associated proteins. We recombinantly produced a protein mimicking the M. galloprovincialis preCol-NG C-terminal flank region. The protein was intrinsically unfolded in solution, even at elevated temperatures. However, upon contact with small unilamellar vesicles (SUVs) reversible β-structure formation occurred, reminiscent of partitioning-folding coupling. This behavior of preCol-NG flank domains likely impacts byssogenesis and sheds new light on a distinct mechanism of how fibrous protein materials might be achieved by lipid-induced self-assembly in nature.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Intrinsically Disordered Proteins / chemistry*
  • Micelles
  • Molecular Mimicry
  • Molecular Sequence Data
  • Mytilus / chemistry*
  • Phospholipids / chemistry*
  • Protein Folding
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Sodium Dodecyl Sulfate / chemistry
  • Surface-Active Agents / chemistry
  • Unilamellar Liposomes / chemistry


  • Intrinsically Disordered Proteins
  • Micelles
  • Phospholipids
  • Surface-Active Agents
  • Unilamellar Liposomes
  • Sodium Dodecyl Sulfate