The present invention relates to a novel process for preparation of peptides having amino acid chain length in the range of 2-40 comprises the steps: i) attaching an end-blocked amino acid with an ionic liquid based solid support in presence of an ionic solvent to obtain an end-terminal blocked amino acid attached ionic liquid; ii) removing end-terminal blocking agent from the end-terminal blocked amino acid attached ionic liquid of step i) followed by work up to obtain an amino acid attached ionic liquid; iii) repeating steps i) through ii) one or more times to obtain a polypeptide attached ionic liquid; and iv) detaching the polypeptide from the polypeptide attached ionic liquid of step iii) to obtain the polypeptide. Said process does not use any auxiliary reagents like dehydrating agent or activating agent. The use of ionic liquids as supports as well as solvents result in the faster kinetics of the process, the separation issues are reduced, and the process has no racemization issues.

The invention discloses a polypeptide compound and a preparation method and application thereof. The polypeptide compound has a structural formula as follows: (X.sub.AX.sub.BX.sub.CX.sub.DX.sub.E-X).sub.2KY, or {(X.sub.AX.sub.BX.sub.CX.sub.DX.sub.E-X).sub.2K}.sub.2KY, or {({X.sub.AX.sub.BX.sub.CX.sub.DX.sub.E-X}.sub.2K).sub.2K}.sub.2KY, where, X.sub.A is a polar amino acid molecule, X.sub.B and X.sub.E are alkaline amino acid molecules (the same or different), X.sub.C and X.sub.D are non-polar amino acid molecules (the same or different), K is lysine (Lys, K), and X and Y are null, or any one or more amino acid or chemical groups. The polypeptide compound provided in the invention has an effect of enhancing the immune function of a body and has an application potential of being developed into a clinical medicine capable of enhancing the immune function of a body.

The invention provides methods of making immune effector cells (e.g., T cells, NK cells) that can be engineered to express a chimeric antigen receptor (CAR), and compositions and reaction mixtures comprising the same.

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.

Disclosed herein are formulations, substrates, and arrays for amino acid and peptide synthesis on microarrays. In certain embodiments, methods for manufacturing and using the formulations, substrates, and arrays including one-step coupling, e.g., for synthesis of peptides in a C.fwdarw.N orientation are disclosed. In some embodiments, disclosed herein are formulations and methods for high efficiency coupling of biomolecules to a substrate.

The present disclosure provides a method of solid-phase peptide synthesis from the N terminus to C terminus without detectable epimerization of the C-terminal amino acid.

A large-scale process is described herein for preparing a cyclic peptide as described, comprising solid phase peptide synthesis of a linear peptide and cleaving it from the resin; oxidizing cysteine residues to form an intramolecular disulfide bond; and isolating the cyclic peptide, wherein: (i) coupling uses diisopropylcarbodiimide and ethyl cyanohydroxyiminoacetate and/or N-hydroxybenzotriazole; (ii) cleaving comprises contacting the peptide with a solution comprising TFA and dithioerythritol and/or dithiothreitol; (iii) the peptide is precipitated after cleaving without prior concentration of the peptide by evaporation; (iv) oxidizing comprises contacting an aqueous solution comprising at least 5 mg/mL peptide with hydrogen peroxide; (v) isolating comprises loading the peptide on a reverse phase chromatography at up to 40 grams/kg column, and elution from the column; (vi) isolating comprises lyophilization, followed by grinding the peptide; and/or (vii) substitution of the resin is at least 0.3 milliequivalents/gram, and/or the resin is a Rink aminomethylstyrene resin.

An object of the present invention is to provide a method for efficiently producing a peptide compound of high purity at a high yield. It was found that an amino acid can be efficiently loaded on a resin for solid-phase synthesis by bringing an amino acid solution containing a specific solvent into contact with a resin for solid-phase synthesis that has been swollen with a specific solvent, thereby solving such problem.

The disclosure is directed to the synthesis and improved methods for purifying macrocyclic peptides produced by solid phase peptide synthesis.

High surface area coatings are applied to solid substrates to increase the surface area available for solid-phase synthesis of polymers. The high surface area coatings use three-dimensional space to provide more area for functional groups to bind polymers than an untreated solid substrate. The polymers may be oligonucleotides, polypeptides, or another type of polymer. The solid substrate is a rigid supportive layer made from a material such as glass, a silicon material, a metal material, and plastic. The coating may be thin films, hydrogels, microparticles. The coating may be made from a metal oxide, a high- dielectric, a low- dielectric, an etched metal, a carbon material, or an organic polymer. The functional groups may be hydroxyl groups, amine groups, thiolate groups, alkenes, n-alkenes, alkalines, N-Hydroxysuccinimide (NHS)-activated esters, polyaniline, aminosilane groups, silanized oxides, oligothiophenes, and diazonium compounds. Techniques for applying coatings to solid substrates and attaching functional groups are also disclosed.