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Heim, Markus ; Elsner, Martina B. ; Scheibel, Thomas:
Lipid-Specific β‑Sheet Formation in a Mussel Byssus Protein Domain.
In: Biomacromolecules.
Bd. 14
(2013)
Heft 9
.
- S. 3238-3245.
ISSN 1526-4602
DOI: https://doi.org/10.1021/bm400860y
Abstract
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 Cterminal
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.