153 results about "Single amino acid" patented technology

The present invention relates to active agent delivery systems and more specifically to compositions that comprise amino acids, as single amino acids or peptides, covalently attached to active agents and methods for administering conjugated active agent compositions.

Interleukin-10 (IL-10) conjugated via a linker to one or more polyethylene glycol (PEG) molecules at a single amino acid residue of the IL-10, and a method for preparing the same, are provided. The method produces a stable mono-pegylated IL-10, which retains IL-10 activity, where pegylation is selective for the N-terminus on one subunit of IL-10 with little or no formation of monomeric IL-10. The method also provides a substantially homogenous population of mono-PEG-IL-10.

The present disclosure provides drug-ligand conjugates that are potent cytotoxins and include a linker between the drug and ligand where the linker has a single amino acid. The disclosure is also directed to compositions containing the drug-ligand conjugates, and to methods of treatment using them.

The invention discloses a preparation method and application for cigarette flavor. The preparation method for the cigarette flavor comprises the following steps: a single amino acid is selected, or a few single amino acids are compounded, and the amino acids are mixed with a saccharide substance according to certain proportion to react under certain conditions to obtain a Maillard reaction liquid product, namely the cigarette flavor. The cigarette flavor obtained by the preparation method has certain improvement on the smoking smell of shredded tobacco, ensures that the smoking fragrance is plumper, reduces smoking miscellaneous gas and the irritation of smoke gas, and improves the sense of comfort.

The present invention provides RecA mutant proteins, having either a single mutation or a double mutation. The RecA mutant proteins are highly proficient in both SSB displacement and steady state binding of DNA in the presence or absence of SSB as compared to the wild-type protein. The single RecA mutant, RecAΔC17, has 17 amino acid residues removed from the carboxyl terminus. The double mutant RecA, RecAΔC17/E38K, combines the 17 amino acid residue C-terminal deletion of RecAΔC17, with a single amino acid change from Glutamate to Lysine at position 38. These RecA mutant proteins are pH sensitive allowing control over formation of products. Hence, methods of using the novel RecA mutants and kits having the RecA mutants as components thereof are also contemplated by the present invention.

Single amino acid compounds and methods for upregulating expression of a gene encoding an antioxidative enzyme, such as superoxide dismutase or catalase, to counteract harmful oxidative effects of reactive oxygen species and other free radicals are described. The single amino acid compounds may be used in compositions and methods to treat or prevent diseases and conditions characterized by undesirable elevation of reactive oxygen species and other free radicals.

The present invention relates to a purified, easily produced poly-beta-1->4-N-acetylglucosamine (p-GlcNAc) polysaccharide species. The p-GlcNAc of the invention is a polymer of high molecular weight whose constituent monosaccharide sugars are attached in a beta-1->4 conformation, and which is free of proteins, and substantially free of single amino acids, and other organic and inorganic contaminants. In addition, derivatives and reformulations of p-GlcNAc are described. The present invention further relates to methods for the purification of the p-GlcNAc of the invention from microalgae, preferably diatom, starting sources. Still further, the invention relates to methods for the derivatization and reformulation of the p-GlcNAc. Additionally, the present invention relates to the uses of pure p-GlcNAc, its derivatives, and/or its reformulations.

An engineered highly specific DNA-cleavage enzyme delivers a site-specific nick in a double stranded DNA, to cleave one DNA strand within its target site while leaving the opposing DNA strand intact. The engineered enzyme provides the ability to induce a gene conversion event in a mammalian cell. An engineered sequence-specific nickase derived from a LAGLIDADG homing endonuclease is altered by a single amino acid residue, wherein the amino acid residue is involved in the polarization of solvent molecules and acid-base catalysis in the active site without affecting direct contacts between the enzyme and either the bound DNA or bound metal ions. Engineered, site-specific nickase variants, such as of I-AniI and other homing endonucleases, are particularly useful in targeted genome engineering as well as therapeutic, targeted gene repair.

The invention relates to a method for preparing Semaglutide through solid and liquid combination, and solves the technical problems that in the process for synthesizing long-sequence polypeptide by the existing technology, the synthesis period is long; the purification difficulty is high; the yield is low. The method for preparing Semaglutide through solid and liquid combination provided by the invention is characterized in that firstly, Lys and resin are condensed in an Alloc-Lys(Fmoc)-OH form by adopting a solid phase synthesis method; Fmoc protecting groups on epsilon-NH2 are removed; sidechain connection is performed; cracking is performed to obtain Alloc-Lys(PEG-PEG-gamma-Glu(OtBu)-Monobutyl octadecanate)-OH; meanwhile, 10 dipeptide or tripeptide or tetrapeptide fragments are simultaneously synthesized by a liquid phase synthesis method; then, the condensation reaction of the synthesized peptide fragments and single amino acid is performed by using the resin as a carrier; the 15-step solid phase condensation reaction is reduced in the process; the generation of lacked peptide impurities is reduced; the product purity and the yield are improved; meanwhile, the generation of the impurities of [+Gly]-Semaglutide and [+Ala]-Semaglutide is effectively avoided; the purification difficulty is greatly reduced. The method is widely applied to the technical field of polypeptide medicine preparation.

The present invention relates to active agent delivery systems and more specifically to compositions that comprise amino acids, as single amino acids or peptides, covalently attached to active agents and methods for administering conjugated active agent compositions.

Synthetic amino acids containing one or more non-fouling groups or moieties are described herein. In one embodiment, the amino acid has the following chemical formula:

where L is a linker group and Z is a non-fouling group including, but not limited to, polyethylene glycol (PEG); oligoethylene glycol (OEG); zwitterionic group, such as phosphorycholine, carboxybetaine, and sulfobetaine; groups that are hydrogen bond acceptors but not hydrogen bond donors. The non-fouling amino acids can be incorporated into a bioactive peptide as single amino acid residues, multiples amino acid residues, or as blocks of amino acids. The non-fouling amino acids, or peptides containing one or more non-fouling amino acids, can be applied to surfaces in order to improve biocompatibility, reduce thrombogenesis, and/or reduce fouling by proteins or bacteria present in solution.

The invention belongs to the technical field of fertilizer production, and specifically discloses an environment-friendly ecological full-nutrient fertilizer and a production method of the fertilizer. The environment-friendly ecological full-nutrient fertilizer comprises raw materials in parts by weight as follows: 10-50 parts of urea, 5-25 parts of ammonium sulfate, 10-40 parts of monoammonium phosphate, 10-40 parts of potassium chloride or potassium sulfate, 5-10 parts of plant straw ash, 1-10 parts of an active nitrogen source, 0.1-0.5 part of an active carbon source and 5-20 parts of a filler, wherein the active nitrogen source is single amino acid or compound amino acid, the active carbon source is a mixture of glucose and vitamin C in a weight ratio of 1: (0.5-4), and the plant straw ash is the straw ash of plants applying the fertilizer. The full-nutrient fertilizer has the characteristics of organic-inorganic combination and environmental protection, the output increase is obvious, and the utilization rate of the fertilizer is increased.

The present invention relates to a purified, easily produced poly-beta-1->4-N-acetylglucosamine (p-GlcNAc) polysaccharide species. The p-GlcNAc of the invention is a polymer of high molecular weight whose constituent monosaccharide sugars are attached in a beta-1->4 conformation, and which is free of proteins, and substantially free of single amino acids, and other organic and inorganic contaminants. In addition, derivatives and reformulations of p-GlcNAc are described. The present invention further relates to methods for the purification of the p-GlcNAc of the invention from microalgae, preferably diatom, starting sources. Still further, the invention relates to methods for the derivatization and reformulation of the p-GlcNAc. Additionally, the present invention relates to the uses of pure p-GlcNAc, its derivatives, and/or its reformulations.

It has been determined that allergens, which are characterized by both humoral (IgE) and cellular (T cell) binding sites, can be modified to be less allergenic by modifying the IgE binding sites. The IgE binding sites can be converted to non-IgE binding sites by masking the site with a compound that prevents IgE binding or by altering as little as a single amino acid within the protein, most typically a hydrophobic residue towards the center of the IgE binding epitope, to eliminate IgE binding. The method allows the protein to be altered as minimally as possible, other than within the IgE-binding sites, while retaining the ability of the protein to activate T cells, and, in some embodiments by not significantly altering or decreasing IgG binding capacity. The examples use peanut allergens to demonstrate alteration of IgE binding sites. The critical amino acids within each of the IgE binding epitopes of the peanut protein that are important to immunoglobulin binding have been determined. Substitution of even a single amino acid within each of the epitopes led to loss of IgE binding. Although the epitopes shared no common amino acid sequence motif, the hydrophobic residues located in the center of the epitope appeared to be most critical to IgE binding.

The present invention relates to active agent delivery systems and more specifically to compositions that comprise amino acids, as single amino acids or peptides, covalently attached to active agents and methods for administering conjugated active agent compositions.