A Short Peptide Hydrogel with High Stiffness Induced by 310-Helices to β-Sheet Transition in Water

Shu Hui Hiew, Harini Mohanram, Lulu Ning, Jingjing Guo, Antoni Sánchez-Ferrer, Xiangyan Shi, Konstantin Pervushin, Yuguang Mu, Raffaele Mezzenga, Ali Miserez

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35 Citations (Scopus)


Biological gels generally require polymeric chains that produce long-lived physical entanglements. Low molecular weight colloids offer an alternative to macromolecular gels, but often require ad-hoc synthetic procedures. Here, a short biomimetic peptide composed of eight amino acid residues derived from squid sucker ring teeth proteins is demonstrated to form hydrogel in water without any cross-linking agent or chemical modification and exhibits a stiffness on par with the stiffest peptide hydrogels. Combining solution and solid-state NMR, circular dichroism, infrared spectroscopy, and X-ray scattering, the peptide is shown to form a supramolecular, semiflexible gel assembled from unusual right-handed 310-helices stabilized in solution by π–π stacking. During gelation, the 310-helices undergo conformational transition into antiparallel β-sheets with formation of new interpeptide hydrophobic interactions, and molecular dynamic simulations corroborate stabilization by cross β-sheet oligomerization. The current study broadens the range of secondary structures available to create supramolecular hydrogels, and introduces 310-helices as transient building blocks for gelation via a 310-to-β-sheet conformational transition.

Original languageEnglish
Article number1901173
JournalAdvanced Science
Issue number21
Publication statusPublished - 1 Nov 2019
Externally publishedYes


  • NMR spectroscopy
  • molecular dynamics (MD) simulations
  • peptide hydrogels
  • suckerin
  • β-sheet transition


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