Supramolecular materials constructed from synthetic glycopeptides aqueous self-assembly and their bioapplications in immunotherapy.

Synthetic glycopeptides capable of self-assembly in aqueous environments form a range of supramolecular nanostructures, such as nanoparticles and nanofibers, owing to their amphiphilic nature and the diverse structures of the saccharides introduced. These glycopeptide-based supramolecular materials are promising for immunotherapy applications because of their biocompatibility and multivalent saccharide display, which enhances lectin-saccharide interactions. This review highlights recent advances in the molecular design of synthetic glycopeptide-based supramolecular materials and their use as immunomodulatory agents.

Oxidation-Responsive Supramolecular Hydrogels Based on Glucosamine Derivatives with an Aryl Sulfide Group.

Supramolecular hydrogels can be obtained via self-assembly of small molecules in aqueous environments. In this study, we describe the development of oxidation-responsive supramolecular hydrogels comprising glucosamine derivatives with an aryl sulfide group. We demonstrate that hydrogen peroxide can induce a gel-sol transition through the oxidation of the sulfide group to the corresponding sulfoxide.

Design of supramolecular hybrid nanomaterials comprising peptide-based supramolecular nanofibers and generated DNA nanoflowers through rolling circle amplification.

The artificial construction of multicomponent supramolecular materials comprising plural supramolecular architectures that are assembled orthogonally from their constituent molecules has attracted growing attention. Here, we describe the design and development of multicomponent supramolecular materials by combining peptide-based self-assembled fibrous nanostructures with globular DNA nanoflowers constructed by the rolling circle amplification reaction. The orthogonally constructed architectures were dissected by fluorescence imaging using the selective fluorescence staining procedures adapted to this study.

Physiological lipid composition is vital for homotypic ER membrane fusion mediated by the dynamin-related GTPase Sey1p.

Homotypic fusion of the endoplasmic reticulum (ER) is required for generating and maintaining the characteristic reticular ER membrane structures. This organelle membrane fusion process depends on the ER-bound dynamin-related GTPases, such as atlastins in animals and Sey1p in yeast. Here, to investigate whether specific lipid molecules facilitate GTPase-dependent ER membrane fusion directly, we comprehensively evaluated membrane docking and lipid mixing of reconstituted proteoliposomes bearing purified Sey1p and a set of ER-mimicking lipids, including phosphatidylcholine, phosphatidylethanolamine, phosphatidylinositol, phosphatidylserine, phosphatidic acid, and ergosterol.