Supramolecular hydrogels formed by self-assembly of low-molecular-weight amphiphiles (hydrogelators) in water via multiple weak non-covalent interactions have attracted considerable attention as functional soft materials. Because the supramolecular hydrogels can immobilise artificial- or bio-molecules under semi-wet conditions without drying or troublesome chemical processes, their application as biomaterials has been actively attempted. In this field, saccharides have been considered as important components of hydrogelators, as they are biocompatible and not only function as hydrophilic groups but also serve as hydrogen bonding sites due to the several hydroxyl groups present in their structure. In this mini-review, recent advances in the use of saccharides in supramolecular hydrogels research are introduced.

Glycoprotein quality control in the endoplasmic reticulum is achieved by multiple molecular chaperones, glycosyltransferases, and glycosidases. Calnexin and calreticulin, which are lectin-type molecular chaperones, play important roles in glycoprotein folding. These chaperones interact with nascent proteins modified with the Glc₁Man₉GlcNAc₂ (G1M9) glycan, leading to the formation of a correct structure. ERp57, a disulfide isomerase family protein, complexes with these chaperones and assists in the formation of disulfide bonds. In recent years, it has been shown that proteins other than ERp57 also complex with chaperones, suggesting that there may be multiple chaperone-binding partner molecules. This review discusses partner proteins interacting with calnexin and calreticulin and their functions. It also recommends further studying the formation of the intracellular complex of CNX/CRT with peptidyl-prolyl cis-trans isomerases and protein disulfide isomerase family proteins in order to understand the involvement of these proteins in glycoprotein quality control mechanism.

Several types of lectin domains that specifically recognize chitin have been discovered in plants. One such domain, the hevein domain, also known as CBM18, contains eight cysteine and glycine residues at conserved positions in 40 amino acid residues. It works alone, arranged in tandem, or in combination with other domains. Tomato lectin is a chimeric lectin composed of four hevein domains and extensin-like domains similar to the plant cell wall glycoprotein extensin. It has been used for tissue staining and the fractionation of sugar chains owing to its specificity against poly-N-acetyllactosamine. In this minireview, the author summarizes the current literature on the chitin-binding lectins of plants and discuss the role of tomato lectin.

Supramolecular hydrogels formed by self-assembly of low-molecular-weight amphiphiles (hydrogelators) in water via multiple weak non-covalent interactions have attracted considerable attention as functional soft materials. Because the supramolecular hydrogels can immobilise artificial- or bio-molecules under semi-wet conditions without drying or troublesome chemical processes, their application as biomaterials has been actively attempted. In this field, saccharides have been considered as important components of hydrogelators, as they are biocompatible and not only function as hydrophilic groups but also serve as hydrogen bonding sites due to the several hydroxyl groups present in their structure. In this mini-review, recent advances in the use of saccharides in supramolecular hydrogels research are introduced.

Glycoprotein quality control in the endoplasmic reticulum is achieved by multiple molecular chaperones, glycosyltransferases, and glycosidases. Calnexin and calreticulin, which are lectin-type molecular chaperones, play important roles in glycoprotein folding. These chaperones interact with nascent proteins modified with the Glc₁Man₉GlcNAc₂ (G1M9) glycan, leading to the formation of a correct structure. ERp57, a disulfide isomerase family protein, complexes with these chaperones and assists in the formation of disulfide bonds. In recent years, it has been shown that proteins other than ERp57 also complex with chaperones, suggesting that there may be multiple chaperone-binding partner molecules. This review discusses partner proteins interacting with calnexin and calreticulin and their functions. It also recommends further studying the formation of the intracellular complex of CNX/CRT with peptidyl-prolyl cis-trans isomerases and protein disulfide isomerase family proteins in order to understand the involvement of these proteins in glycoprotein quality control mechanism.

Several types of lectin domains that specifically recognize chitin have been discovered in plants. One such domain, the hevein domain, also known as CBM18, contains eight cysteine and glycine residues at conserved positions in 40 amino acid residues. It works alone, arranged in tandem, or in combination with other domains. Tomato lectin is a chimeric lectin composed of four hevein domains and extensin-like domains similar to the plant cell wall glycoprotein extensin. It has been used for tissue staining and the fractionation of sugar chains owing to its specificity against poly-N-acetyllactosamine. In this minireview, the author summarizes the current literature on the chitin-binding lectins of plants and discuss the role of tomato lectin.