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|Title:||Squid suckerin biomimetic peptides form amyloid-like crystals with robust mechanical properties||Authors:||Hiew, Shu Hui
|Issue Date:||2017||Source:||Hiew, S. H., Sánchez-Ferrer, A., Amini, S., Zhou, F., Adamcik, J., Guerette, P., et al. (2017). Squid Suckerin Biomimetic Peptides Form Amyloid-like Crystals with Robust Mechanical Properties. Biomacromolecules, 18(12), 4240-4248.||Series/Report no.:||Biomacromolecules||Abstract:||We present the self-assembly of fibers formed from a peptide sequence (A1H1) 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. A1H1 displays amphiphilic characteristics and self-assembles from the bottom-up into mm-scale fibers initiated by the addition of a polar aprotic solvent. A1H1 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.||URI:||https://hdl.handle.net/10356/86572
|ISSN:||1525-7797||DOI:||10.1021/acs.biomac.7b01280||Rights:||© 2017 American Chemical Society.||Fulltext Permission:||none||Fulltext Availability:||No Fulltext|
|Appears in Collections:||MSE Journal Articles|
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