The present invention has an object of shortening the process time and reducing use of a poor solvent for solidifying a carrier (Tag)-peptide component, by removing impurities without conducting solid-liquid separation (condensation, solid-liquid separation and drying operation) of a Tag-peptide component, in an Fmoc method using a Tag for liquid phase peptide synthesis. Provided is the peptide synthesis method that includes the following steps a-d: step a: a carrier-protected amino acid, carrier-protected peptide, or a carrier-protected amino acid amide, and an N-Fmoc-protected amino acid or an N-Fmoc-protected peptide are condensed in an organic solvent or a mixed solution of organic solvents, to obtain an N-Fmoc-carrier-protected peptide, step b: a water-soluble amine is added to the reaction solution after the condensation reaction, step c: the Fmoc group is deprotected from the protected amino group in the presence of a water-soluble amine, and step d: the reaction solution is neutralized by adding an acid, and further, by adding and washing with an acidic aqueous solution, then, by liquid-liquid separation an aqueous layer is removed to obtain an organic layer.

The present disclosure relates to lipoprotein complexes and lipoprotein populations and their use in the treatment and/or prevention of dyslipidemic diseases, disorders, and/or conditions. The disclosure further relates to recombinant expression of apolipoproteins, purification of apolipoproteins, and production of lipoprotein complexes using thermal cycling-based methods.

A method for preparing peptides is disclosed, the method comprising a step of forming a peptide bond wherein the carboxyl group of a first amino acid or first peptide is activated and an amino group of the first activated amino acid or first peptide is protected by a protecting group having a water-solubility enhancing group and the activated carboxyl group of the first amino acid or first peptide is reacted with an amino group of a second amino acid or second peptide wherein said carboxyl group of the first amino acid or first peptide is activated in the absence of the second amino acid or second peptide. Peptides comprising a protecting group having a water-solubility enhancing group being bound to the amino group and an activated or free carboxyl group are also disclosed.

Described are affinity purification system that includes a carrier/surface that is non-cellular, and sliding clamp (SC) protein, and methods for purifying proteins that bind to the SC. The SC is associated with the carrier/surface via covalent/non-covalent interactions. To attain control of coupling site, the SC can be mutated via site-directed mutagenesis to introduce an exogenous residue and, the exogenous internal residue is conjugated to the non-cellular surface through the linker. The SC can also be coupled to the carrier via non-covalent interactions such as the affinity interactions involved in ligand/binding partner complex formation.

The SC-based affinity purification system are used in a purification column as bait proteins, to isolate SC binding partners or non SC-binding proteins engineered to contain a SC binding site prior to its purification.

The present disclosure provides computer-based methods and systems for controlling peptide synthesis. An embodiment begins by providing a manufacturing process that synthesizes peptides using solid phase slug flow. In turn, the manufacturing process is automated through use of a machine learning engine by selecting values for operating conditions for the manufacturing process. In such an embodiment, a given operating condition is flow rate profile. An embodiment generates an indication of the selected values for the operating conditions and controls the manufacturing process therewith.

The present disclosure provides efficient and reliable methods for preparing cyclized peptidic compounds. Advantageously, the currently described methods allow for on-resin cyclization using a limited number of processing steps, while increasing the chemical diversity available for the cyclized peptidic compounds produced.

The present invention refers to a method for preparing a glucagon-like peptide, comprising precipitation of the peptide or of a precursor peptide by means of mixing with an anti-solvent comprising diisopropyl ether and acetonitrile. Further, the present invention also relates to a peptide conjugated to a solid phase and a pharmaceutical composition comprising a Liraglutide peptide obtainable from a method according to the present invention.

The invention relates to a compound or a salt thereof, a method for preparation thereof, and use thereof, wherein the compound has the structure of Formula (1):

##STR00001## the substituents in Formula (1) are as defined in the specification. The compound of Formula (1) or a salt thereof can be attached to a solid-phase resin, on which solid-phase synthesis may be performed.

Systems and processes for performing solid phase peptide synthesis are generally described. Solid phase peptide synthesis is a known process in which amino acid residues are added to peptides that have been immobilized on a solid support. In certain embodiments, the inventive systems and methods can be used to perform solid phase peptide synthesis quickly while maintaining high yields. Certain embodiments relate to processes and systems that may be used to heat, transport, and/or mix reagents in ways that reduce the amount of time required to perform solid phase peptide synthesis.

Systems and processes for performing solid phase peptide synthesis are generally described. Solid phase peptide synthesis is a known process in which amino acid residues are added to peptides that have been immobilized on a solid support. In certain embodiments, the inventive systems and methods can be used to perform solid phase peptide synthesis quickly while maintaining high yields. Certain embodiments relate to processes and systems that may be used to heat, transport, and/or mix reagents in ways that reduce the amount of time required to perform solid phase peptide synthesis.