TY - JOUR
T1 - A Short Peptide Hydrogel with High Stiffness Induced by 310-Helices to β-Sheet Transition in Water
AU - Hiew, Shu Hui
AU - Mohanram, Harini
AU - Ning, Lulu
AU - Guo, Jingjing
AU - Sánchez-Ferrer, Antoni
AU - Shi, Xiangyan
AU - Pervushin, Konstantin
AU - Mu, Yuguang
AU - Mezzenga, Raffaele
AU - Miserez, Ali
N1 - Publisher Copyright:
© 2019 The Authors. Published by WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
PY - 2019/11/1
Y1 - 2019/11/1
N2 - 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.
AB - 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.
KW - NMR spectroscopy
KW - molecular dynamics (MD) simulations
KW - peptide hydrogels
KW - suckerin
KW - β-sheet transition
UR - http://www.scopus.com/inward/record.url?scp=85072216555&partnerID=8YFLogxK
U2 - 10.1002/advs.201901173
DO - 10.1002/advs.201901173
M3 - Article
AN - SCOPUS:85072216555
SN - 2198-3844
VL - 6
JO - Advanced Science
JF - Advanced Science
IS - 21
M1 - 1901173
ER -