Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/86572
Title: Squid suckerin biomimetic peptides form amyloid-like crystals with robust mechanical properties
Authors: Hiew, Shu Hui
Sánchez-Ferrer, Antoni
Amini, Shahrouz
Zhou, Feng
Adamcik, Jozef
Guerette, Paul
Su, Haibin
Mezzenga, Raffaele
Miserez, Ali
Keywords: Bioinformatics
Peptides
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
http://hdl.handle.net/10220/45172
ISSN: 1525-7797
DOI: http://dx.doi.org/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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