A method of preparing extracellularly assembled higher order antigen from a native lower order antigen the method comprising the following steps: (i) contacting lower order antigen with a solution comprising a reducing agent for a time and under 5 conditions sufficient to reduce one or more native cysteines; and (ii) removing or diluting the reducing agent or contacting the reduced lower order antigen with an oxidising agent, to elicit assembly of lower order antigen from (i) into an assembled higher order antigen; wherein at least 10% of the lower order antigen is converted to higher order antigen in step (ii) and whereby the assembled higher order antigen 10 displays at least reduced binding to non-neutralizing antibodies compared to the lower order antigen and retains binding to at least one neutralizing antibody. A method of producing a vaccine composition comprising following the steps of the method and then mixing the assembled higher order antigen with a pharmaceutically or physiologically acceptable diluent, carrier or adjuvant. A composition comprising a 15 higher order extracellularly assembled antigen, wherein the assembled antigen displays at least reduced binding to a non-neutralizing antibody compared to a native control higher order antigen. Use of the assembled higher order antigen to stimulate an immune response or for the detection and/or isolation of an immune cell such as a B-cell specific for the antigen.

The invention provides a ternary complex of a cucurbituril host, such as CB[8], with a first aryl guest and second aryl guest, wherein the first aryl guest is a group within a biomolecule, such as insulin, and the first and second aryl guests are different. Also provided is a method of decomplexing the complex, the method comprising the step of treating the complex with a competitor guest, and permitting the competitor guest to displace at least the first aryl guest from the complex.

This application describes modified amino acids and polypeptides comprising a SO.sub.2F or CH.sub.2CH.sub.2SO.sub.2F group bound to the side chain of an amino acid or amino acid residue of a polypeptide in place of a hydrogen of a hydroxyl or amino substituent thereof. Methods of covalently binding the polypeptides to receptor sites of receptor proteins are also described herein.

The present invention relates to a method for preparing an in vitro evolution-based hotspot-derived peptide-nucleic acid hybrid molecule. According to the method of the present invention, a hotspot-derived peptide-nucleic acid hybrid molecule that can bind with high affinity to viruses and effectively block the binding between the virus and the receptor can be rapidly prepared and screened in response to various virus mutations among numerous candidates. Therefore, it can be used very effectively for the development of therapeutics against various viral mutations.

The present invention provides a method for producing a refolded protein, the method comprising a step for mixing, inside a micro mixer, a buffer and a solubilization solution for a protein that has lost higher order structure or that has become insoluble.

The present disclosure relates to a system for a composition for protein denaturation. The composition includes a non-nucleophilic denaturant comprising a substituted guanidine, wherein the denaturant has a pKa value greater than about 10, and wherein the concentration of the substituted guanidine is less than 250 mM.