A bio-nanocompound incorporating metal oxide particles as substrate, an amino organosilane as linker, a dialdehyde as crosslinking agent and a nucleation agent that utilizes ice nucleating activity to create ice on low energy demand at temperatures down to 0° C. and extend cold chains without increasing energy consumption, wherein even the first application is capable of freezing to different shapes and volumes; a method for producing the bio-nanocompound by self-assembly technique, by mixing the substrate, immobilizing the linker on the substrate, immobilizing the crosslinker on the linker and immobilizing by covalent bonding nucleating agent on the crosslinker; and a coolant having the bio-nanocompound.

A method for self-assembly of a protein in a three-dimensional honeycomb structure, comprising the following consecutive steps: providing a solution comprising a solvent and a protein, the protein comprising a sequence of amino acids corresponding to an oligomerisation domain of a LEAFY protein, for example to the oligomerisation domain of Ginkgo biloba, in fusion with a tag, placing the solution in contact with a substrate, evaporating the solvent in order to crystallise the protein, the oligomerisation domain crystallising in the form of a primary helix, each primary helix interacting with six other primary helixes, whereby a three-dimensional honeycomb protein structure is obtained perpendicular to the substrate, the protein structure being attached to the substrate by the tag.

A method for self-assembly of a protein in a three-dimensional honeycomb structure, comprising the following consecutive steps: providing a solution comprising a solvent and a protein, the protein comprising a sequence of amino acids corresponding to an oligomerisation domain of a LEAFY protein, for example to the oligomerisation domain of Ginkgo biloba, in fusion with a tag, placing the solution in contact with a substrate, evaporating the solvent in order to crystallise the protein, the oligomerisation domain crystallising in the form of a primary helix, each primary helix interacting with six other primary helixes, whereby a three-dimensional honeycomb protein structure is obtained perpendicular to the substrate, the protein structure being attached to the substrate by the tag.

The present invention provides a lectin-magnetic carrier coupling complex for separating glycosylated exosomes from a clinical sample. The lectin-magnetic carrier coupling complex comprises a magnetic carrier and lectins coupled to the outer side of the magnetic carrier. The lectin-magnetic carrier coupling complex provided by the present invention may rapidly, accurately, and automatically separate glycosylated exosomes from a clinical sample with a high separation efficiency; and the separated exosomes are intact in morphology without rupturing or cracking, may be directly used for liquid detection of glycosylated exosomes, or directly used for immunology-related detection, or directly used for nucleotide sequence detection and analysis after extracting nucleic acids from the exosomes.

A polypeptide, a photoresist composition including the polypeptide, a photoresist including the polypeptide, and a method of forming patterns using the photoresist composition.

Provided in this disclosure are chimeric peptides that include a spacer domain, the spacer domain itself, substrates (e.g., implants) coated with the chimeric peptides, and methods for making and using the coated substrates.

The invention provides an oriented and covalent method for immobilizing a glycoprotein and an antibody on a chip. The method includes providing a silver-coated solid surface equipped with alkynes and cuprous oxide nanoparticles. The azido boronic acid tosyl probe is conjugated to the silver-coated solid surface by the cuprous oxide nanoparticles through the self-catalyzed azide-alkyne cycloaddition reaction. The glycan(s) of a glycoprotein or an antibody is provided to the boronic acid tosyl probe, and alcohol groups of the glycan(s) of the glycoprotein or the antibody and the boronic acid group of boronic acid tosyl probe form boronate ester. The nucleophilic residues on the glycoprotein or the antibody replace the tosyl group by SN2 reaction, so as to immobilize the glycoprotein or the antibody through the covalent bond formation.

The invention provides an oriented and covalent method for immobilizing a glycoprotein and an antibody on a chip. The method includes providing a silver-coated solid surface equipped with alkynes and cuprous oxide nanoparticles. The azido boronic acid tosyl probe is conjugated to the silver-coated solid surface by the cuprous oxide nanoparticles through the self-catalyzed azide-alkyne cycloaddition reaction. The glycan(s) of a glycoprotein or an antibody is provided to the boronic acid tosyl probe, and alcohol groups of the glycan(s) of the glycoprotein or the antibody and the boronic acid group of boronic acid tosyl probe form boronate ester. The nucleophilic residues on the glycoprotein or the antibody replace the tosyl group by SN2 reaction, so as to immobilize the glycoprotein or the antibody through the covalent bond formation.

An antimicrobial agent comprising a selenium nanoparticle (SeNP) core and one or more superficially located antimicrobial peptide/s (AMP). The or each AMP may comprise an excess of positively charged amino acids compared to negatively charged amino acids and the AMP may comprise peptides from classes selected from polylysine, such as ε-poly-L-lysine (ε-PL), polyarginine, aurein, ovispirin, melittin, magainin, cecropin, andropin, moricin, ceratotoxin, melittin, magainin, dermaseptin, bombinin, brevinin, esculentins, buforin, cathelicidin, abaecin, apidaecin, prophenin and indolicidin. Products comprising such agents, methods of producing the agents and methods of killing or retarding growth of microorganisms exposed to the agents are also disclosed.

An antimicrobial agent comprising a selenium nanoparticle (SeNP) core and one or more superficially located antimicrobial peptide/s (AMP). The or each AMP may comprise an excess of positively charged amino acids compared to negatively charged amino acids and the AMP may comprise peptides from classes selected from polylysine, such as ε-poly-L-lysine (ε-PL), polyarginine, aurein, ovispirin, melittin, magainin, cecropin, andropin, moricin, ceratotoxin, melittin, magainin, dermaseptin, bombinin, brevinin, esculentins, buforin, cathelicidin, abaecin, apidaecin, prophenin and indolicidin. Products comprising such agents, methods of producing the agents and methods of killing or retarding growth of microorganisms exposed to the agents are also disclosed.