The present invention is broadly concerned with new in vitro glycosylation methods that provide rational approaches for producing glycosylated proteins, and the use of glycosylated proteins. In more detail, the present invention comprises methods of glycosylating a starting protein having an amino sidechain with a nucleophilic moiety, comprising the step of reacting the protein with a carbohydrate having an oxazoline moiety on the reducing end thereof, to covalently bond the amino sidechain of the starting protein with the oxazoline moiety, wherein the glycosylated protein substantially retains the structure and function of the starting protein. Target proteins include oxidase, oxidoreductase and dehydrogenase enzymes. The glycosylated proteins advantageously have molecular weights of at least about 7500 Daltons. In a further embodiment, the present invention concerns the use of glycosylated proteins, fabricated by the methods disclosed herein, in the assembly of amperometric biosensors.

A method for specific linkage to a glycoprotein includes obtaining a glycoprotein having a monoglycan or diglycan attached thereto; producing a reactive functional group on a sugar unit on the glycoprotein; and coupling a linker or a payload to the reactive functional group on the glycoprotein.

This document relates to conjugates of TNF inhibitors or derivatives thereof and functionalized (e.g., mono- or bi-functional) polymers (e.g., polyethylene glycol and related polymers) as well as methods and materials for making and using such conjugates.

The present disclosure relates to compounds and methods for selective C-terminal functionalization of peptides. In certain embodiments, the compounds have improved water-solubility, and are suitable for use in connection with peptide sequencing methodologies.

The present disclosure provides for bioconjugation of biomolecules with functionalized trans-cyclooctenes (TCOs).

There is provided a peptide-containing compound that comprises a peptide component which is an amino acid sequence of from 2 to 45 (e.g. from 6 to 15) amino acids, which peptide component is covalently bonded to one or more compounds of formula I: ##STR00001##
wherein: R.sup.1 is selected from the group consisting of —C(CH.sub.3).sub.2OH, —COCH.sub.3, —C(CH.sub.3)═CH.sub.2 and —C(CH.sub.3).sub.2H; and n is 0, 1 or 2,
as well as regioisomers, stereoisomers, and pharmaceutically- or cosmetically-acceptable salts of said peptide-containing compound. The compound of formula I is preferably montelukast, montelukast styrene or hydrogenated montelukast styrene. The peptide-containing compound is particularly useful in the treatment of conditions characterised by inflammation, including wounds, hemorrhoids, burns, psoriasis, acne, atopic dermatitis, allergic rhinitis, allergic conjunctivitis, chronic obstructive pulmonary disease, inflammatory bowel disease (such as ulcerative colitis). Compounds of the invention are also useful in the treatment of idiopathic pulmonary fibrosis.

This document relates to conjugates of a biologically active molecule or a derivative thereof and functionalized (e.g., mono- or bi-functional) polymers (e.g., polyethylene glycol and related polymers) as well as methods and materials for making and using such conjugates.

The present disclosure provides methods of preparing heteroaryl-containing compounds, wherein an azide-alkyne cycloaddition is accelerated in the presence of lauryldimethylamine oxide (LDAO). The present disclosure further provides conjugates of polypeptides and antigens prepared using such methods.

The present invention relates to a stapled peptide, a preparation method thereof and the use thereof, and more specifically to an amphipathic alpha-helical stapled peptide comprising hydrophobic amino acids and hydrophilic amino acids, a preparation method thereof, and the use thereof for intracellular delivery of an active substance.

Described herein are methods, compositions and kits utilizing heterogeneous metal catalysts for the preparation of cycloaddition compounds, such as triazoles and biomolecules.