Open AccessA Short Peptide Hydrogel with High Stiffness Induced by 3 10 ‐Helices to β‐Sheet Transition in Water
Author(s) -
Hiew Shu Hui,
Mohanram Harini,
Ning Lulu,
Guo Jingjing,
SánchezFerrer Antoni,
Shi Xiangyan,
Pervushin Konstantin,
Mu Yuguang,
Mezzenga Raffaele,
Miserez Ali
Publication year - 2019
Publication title -
advanced science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.388
H-Index - 100
ISSN - 2198-3844
DOI - 10.1002/advs.201901173
Subject(s) - antiparallel (mathematics) , self healing hydrogels , circular dichroism , supramolecular chemistry , beta sheet , peptide , crystallography , chemistry , self assembly , dynamic light scattering , materials science , nanotechnology , polymer chemistry , nanoparticle , organic chemistry , crystal structure , biochemistry , physics , quantum mechanics , magnetic field
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 3 10 ‐helices stabilized in solution by π–π stacking. During gelation, the 3 10 ‐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 3 10 ‐helices as transient building blocks for gelation via a 3 10 ‐to‐β‐sheet conformational transition.