A Unique Temperature-Induced Reverse Supramolecular Chirality-Assisted Gel-to-Gel Transition.

Supramolecular hydrogels typically undergo a gel-to-sol transition with heat, as intermolecular interactions within the gel weaken. Although gel-to-gel transitions during heating are rare, they may occur due to minor rearrangements caused by thermal forces in the supramolecular self-assembled structure. Here, an unprecedented temperature-induced gel-to-gel transition assisted by supramolecular chiral inversion in a hydrogel system is presented. The transition results from a left-handed M-type helix to a right-handed P-type helix, attributed to the π-system-conjugated amino acid, l-Tyrosine (Fm- l-Tyr). Upon solvent dilution, Fm-l-Tyr induces translucent hydrogel formed by entangled fibers with a kinetically stable left-handed M-type supramolecular helix. At 70 °C, hydrogel transforms into an opaque gel with a reverse supramolecular chirality yielding a thermodynamically stable right-handed P-type helix. Supramolecular chiral inversion is substantiated by two chiroptical methods. This unique gel-to-gel transition, accompanied by chiral inversion, is anticipated to attract attention, especially for applications sensitive to chirality.

π-System Functionalization Transforms Amyloidogenic Peptide Fragment of Human Islet Amyloid Polypeptide into a Super Hydrogelator.

While a considerable number of ultra-short/short amyloid peptides have been reported to form 3D supramolecular hydrogels, they all possess high minimum gelation concentration (MGC) (≥1 wt%), which preclude their applications. In this context, we demonstrate that functionalisation of a well-known amyloidogenic ultra-short peptide fragment NFGAIL (IAPf) of human Islet amyloid polypeptide with a π-system (Fluorenyl, Fm) at the N-terminus of the peptide (Fm-IAPf) yield not only highly thermostable hydrogel at physiological pH but also exhibited super gelator nature as the MGC (0.08 wt%) falls below 0.1 wt%. Various experimental results confirmed that aromatic π-π interactions from fluorenyl moieties and hydrogen bonding interactions between the IAPf drive the self-assembly/fibril formation. Fm-IAPf is the first super hydrogelator derived from amyloid-based ultra-short peptides, to the best of our knowledge. We strongly believe that this report, i. e., functionalization of an amyloid peptide with π-system, provides a lead to develop super hydrogelators from other amyloid-forming peptide fragments for their potential applications.

A "self-shrinking" supramolecular hydrogel with a 3D shape memory performance from an unnatural amino acid derivative.

A supramolecular hydrogel with 3D self-shrinking, without any assistance, and a shape memory performance at room temperature is discovered from an unnatural amino acid derivative, i.e. fluorenylmethoxycarbonyl-L-ß-phenylalanine, as a minimalistic model. The self-shrinking properties of this hydrogel can be explored for potential applications.