Dataset Information

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

ABSTRACT: 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 ?-? stacking. During gelation, the 310-helices undergo conformational transition into antiparallel ?-sheets with formation of new interpeptide hydrophobic interactions, and molecular dynamic simulations corroborate stabilization by cross ?-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-?-sheet conformational transition.

SUBMITTER: Hiew SH

PROVIDER: S-EPMC6839752 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature

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Publications

A Short Peptide Hydrogel with High Stiffness Induced by 3<sub>10</sub>-Helices to β-Sheet Transition in Water.

Hiew Shu Hui SH Mohanram Harini H Ning Lulu L Guo Jingjing J Sánchez-Ferrer Antoni A Shi Xiangyan X Pervushin Konstantin K Mu Yuguang Y Mezzenga Raffaele R Miserez Ali A

Advanced science (Weinheim, Baden-Wurttemberg, Germany) 20190910 21

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 hydro ...[more]

PMID: 31728282

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Project description:Silkworm silk has been widely used as a textile fiber, as biomaterials and in optically functional materials due to its extraordinary properties. The ?-sheet-rich natural nanofiber units of about 10-50 nm in diameter are often considered the origin of these properties, yet it remains unclear how silk self-assembles into these hierarchical structures. A new system composed of ?-sheet-rich silk nanofibers about 10-20 nm in diameter is reported here, where these nanofibers formed into "flowing hydrogels" at 0.5-2% solutions and could be transformed back into the solution state at lower concentrations, even with a high ?-sheet content. This is in contrast with other silk processed materials, where significant ?-sheet content negates reversibility between solution and solid states. These fibers are formed by regulating the self-assembly process of silk in aqueous solution, which changes the distribution of negative charges while still supporting ?-sheet formation in the structures. Mechanistically, there appears to be a shift toward negative charges along the outside of the silk nanofibers in our present study, resulting in a higher zeta potential (above -50 mV) than previous silk materials which tend to be below -30 mV. The higher negative charge on silk nanofibers resulted in electrostatic repulsion strong enough to negate further assembly of the nanofibers. Changing silk concentration changed the balance between hydrophobic interactions and electrostatic repulsion of ?-sheet-rich silk nanofibers, resulting in reversible hydrogel-solution transitions. Furthermore, the silk nanofibers could be disassembled into shorter fibers and even nanoparticles upon ultrasonic treatment following the transition from hydrogel to solution due to the increased dispersion of hydrophobic smaller particles, without the loss of ?-sheet content, and with retention of the ability to transition between hydrogel and solution states through reversion to longer nanofibers during self-assembly. These reversible solution-hydrogel transitions were tunable with ultrasonic intensity, time, or temperature.

Dataset Information

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

Publications

A Short Peptide Hydrogel with High Stiffness Induced by 3<sub>10</sub>-Helices to β-Sheet Transition in Water.

Similar Datasets

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