Abstract: The present invention relates to a composition for preventing, ameliorating, or treating neurological diseases related to copper metabolism, wherein the composition comprises a multi-copper oxidase peptide. A multi-copper oxidase-derived peptide according to the present invention was found to be highly effective for treating myelination damage in the nervous system in a copper-induced neurological disease model, thus indicating that the multi-copper oxidase-derived peptide according to the present invention has a significant therapeutic effect on neurological diseases. Therefore, the multi-copper oxidase-derived peptide can be used in various ways in the field of preventing, ameliorating, and treating neurological diseases.

Abstract: The present invention relates to a composition for the prevention, amelioration, or treatment of urination-related disases, comprising cephalotocin. The cephalotocin according to the present invention modulates oxytocin receptors and vasopressin receptors, and has the effect of reducing urine volume by promoting water reabsorption in the kidneys. This means that cephalotocin has a significant antidiuretic effect, and thus, the cephalotocin of the present invention can be variously used in the field of prevention, amelioration, or treatment of urinary disorders or urination-related diseases.

Abstract: The present invention relates to an Octopus minor-specific octopressin peptide comprising the amino acid sequence of SEQ ID NO: 3, and the peptide, by promoting the brooding behaviors of mother Octopus minor to protect her eggs, may increase the hatched larva rate when applied to partial cultivation of octopuses, and thus may be used for the growth of octopus resources.

Abstract: A method of preparing an antiviral Grateloupia chiangii-derived lectin, includes preparing a crude extract of Grateloupia chiangii that is a red alga; and purifying a Grateloupia chiangii-derived lectin (GLC) from the crude extract by means of electrophoresis using D-mannose affinity chromatography. The present invention is expected to be useful in the field of medicine and pharmaceuticals in the future by identifying an amino acid sequence of the purified lectin and a complementary base sequence coding for the purified lectin.

Abstract: Provided is a recombinant BPL3 protein having ?-GlcNAc-Sp and a glycan binding specificity, the recombinant BPL3 protein produced by synthesizing a recombinant BPL3 (rBPL3) gene encoding a Bryopsis plumosa lectin (BPL3) protein; preparing a tandem repeat rBPL3 gene including a repeating structure of the rBPL3 gene by tandemly binding the rBPL3 genes through spacers; preparing a recombinant plasmid by inserting the tandem repeat rBPL3 gene into an expression vector; and transforming an expression host by the recombinant plasmid. According to the method, the expression efficiency of the recombinant lectin is maximized and the activity of the manufactured recombinant lectin is enhanced.

Abstract: Provided is a method of manufacturing a recombinant BPL3 protein comprising: synthesizing a recombinant BPL3 (rBPL3) gene encoding a Bryopsis plumosa lectin (BPL3) protein; preparing a tandem repeat rBPL3 gene including a repeating structure of the rBPL3 gene by tandemly binding the rBPL3 genes through spacers; preparing a recombinant plasmid by inserting the tandem repeat rBPL3 gene into an expression vector; and transforming an expression host by the recombinant plasmid. According to the method, it is possible to maximize expression efficiency of the recombinant lectin and enhance the activity of the manufactured recombinant lectin.

Abstract: Provided is a method of manufacturing a recombinant BPL3 protein comprising: synthesizing a recombinant BPL3 (rBPL3) gene encoding a Bryopsis plumosa lectin (BPL3) protein; preparing a tandem repeat rBPL3 gene including a repeating structure of the rBPL3 gene by tandemly binding the rBPL3 genes through spacers; preparing a recombinant plasmid by inserting the tandem repeat rBPL3 gene into an expression vector; and transforming an expression host by the recombinant plasmid. According to the method, it is possible to maximize expression efficiency of the recombinant lectin and enhance the activity of the manufactured recombinant lectin.