1 research outputs found
Squid Suckerin Biomimetic Peptides Form Amyloid-like Crystals with Robust Mechanical Properties
We
present the self-assembly of fibers formed from a peptide sequence
(<b>A1H1</b>) derived from suckerin proteins of squid sucker
ring teeth (SRT). SRT are protein-only biopolymers with an unconventional
set of physicochemical and mechanical properties including high elastic
modulus coupled with thermoplastic behavior. We have identified a
conserved peptide building block from suckerins that possess the ability
to assemble into materials with similar mechanical properties as the
native SRT. <b>A1H1</b> displays amphiphilic characteristics
and self-assembles from the bottom-up into mm-scale fibers initiated
by the addition of a polar aprotic solvent. <b>A1H1</b> fibers
are thermally resistant up to 239 °C, coupled with an elastic
modulus of ∼7.7 GPa, which can be explained by the tight packing
of β-sheet-enriched crystalline building blocks as identified
by wide-angle X-ray scattering (WAXS), with intersheet and interstrand
distances of 5.37 and 4.38 Å, respectively. A compact packing
of the peptides at their Ala-rich terminals within the fibers was
confirmed from molecular dynamics simulations, and we propose a hierarchical
model of fiber assembly of the mature peptide fiber