10 results about "Solid-Phase Synthesis Techniques" patented technology

This application discloses a linker and its preparation method. The linker includes pharmacophore P, pharmacophore Q, and deoxynucleotides and / or deoxynucleotide derivatives connecting pharmacophore P and pharmacophore Q. Pharmacophore P is obtained by removing the protecting group from group B, and pharmacophore Q is obtained by removing the protecting group from group X. Group B is obtained by chemically modifying the benzylquinolone carboxylic acid pharmacophore, and group X is obtained by chemically modifying the zenomeprazole pharmacophore. The linker is prepared by linking group B and group X with deoxynucleotides and / or deoxynucleotide derivatives to form the linker, including solid-phase synthesis technology. The method of this application can automatically synthesize molecular probes or bivalent drugs containing two pharmacophores, thereby replacing the traditional stepwise linking method, enabling efficient construction of screening libraries, and allowing control of the spatial distance and spatial orientation of the pharmacophores by adjusting the number and base arrangement of deoxynucleotides.

The invention belongs to the technical field of low-temperature solid-phase synthesis, and particularly relates to a microwave-assisted low-temperature solid-phase synthesis method and device. The microwave-assisted low-temperature solid-phase synthesis method comprises the following steps: placing a reaction cavity of a spiral gas-solid two-phase flow reactor in a microwave-assisted heating system, and applying a microwave heating field to the reaction system in the reaction cavity by adopting a microwave generator; under the condition of a microwave heating field, carrier gas and feed gas are introduced into the spiral gas-solid two-phase flow reactor by using compressed gas, and the feed gas brings materials into a reaction cavity for continuous low-temperature solid-phase synthesis reaction. The microwave-assisted heating system is used for carrying out assisted heating on the reaction system, so that the reaction time for preparing various materials is shortened, and the synthesis efficiency of the materials is improved; moreover, the mass and heat transfer efficiency in the low-temperature solid-phase reaction process is improved, the reaction time of each material is shortened, and the purity and yield of a target product are improved.

The invention discloses an H-phosphonate solid-phase connexon, a preparation method thereof and application of the H-phosphonate solid-phase connexon in solid-phase flow synthesis of circular nucleic acid. According to the preparation method, a solid-phase synthesis technology is adopted, exposed amino resin and succinic anhydride are subjected to a condensation reaction to obtain a solid-phase carrier with carboxylic acid, then the solid-phase carrier and 5 '-O-(4, 4'-dimethoxytriphenylmethyl) deoxycytidine are subjected to an amidation reaction under the assistance of a condensing agent and a condensation activating agent, loading of deoxycytidine is achieved, and finally H-phosphonation of hydroxyl is completed. The H-phosphonate solid-phase linker is obtained. The linker disclosed by the invention can realize cyclization closure of a linear precursor by utilizing an efficient reaction between an H-phosphonate group and a terminal hydroxyl group of the linker. The synthesis strategy has the remarkable advantages that the cyclization process can be completed only in 6 hours, and the separation yield reaches up to 73%. The whole process condition is mild, the operation is simple and convenient, the reaction is rapid, and the gram-scale preparation of the cyclic nucleic acid can be efficiently realized.

The invention discloses nonapeptide for dispelling effects of alcohol and protecting liver and a preparation method thereof, and belongs to the technical field of biology. The abbreviation of the nonapeptide is NNYNLPILR, the molecular weight of the nonapeptide is 1116.30, and the sequence of the nonapeptide is as follows: Asn-Asn-Tyr-Asn-Leu-Pro-Ile-Leu-Arg. The method comprises the following steps: selecting macromolecular resin, according to the characteristics of an amino acid sequence Asn-Asn-Tyr-Asn-Leu-Pro-Ile-Leu-Arg, connecting a hydroxyl group of Arg with the resin, then carrying out a shrinkage reaction and treatment on an amino group of Leu and a carboxyl group of Arg, then adding Ile, carrying out a reaction on an amino group of Ile and a carboxyl group of Leu, sequentially adding amino acids from right to left, adding the last Asn amino acid, and then cutting off the resin to obtain the target polypeptide. According to the invention, China-hemp seed protein is taken as a raw material, a biological enzymolysis technology is combined with bioinformatics and a molecular docking technology to screen nonapeptide with alcohol dehydrogenase activation activity, and polypeptide synthesis and in-vitro activity determination are carried out through a solid-phase synthesis technology. The polypeptide with the hemp seed protein source capable of activating the activity of ethanol dehydrogenase is obtained and can be used for developing medicines with the functions of dispelling the effects of alcohol and protecting the liver.

This invention discloses the preparation and application of a base-sensitive linker arm for solid-phase synthesis of polysaccharides, belonging to the fields of glycochemistry and solid-phase synthesis technology. This invention provides a base-sensitive linker arm system comprising an ester core, a linker, and a solid-phase support; one end of the ester core is connected to the solid-phase support, and the other end is connected to the linker; one end of the linker is connected to the ester core, and the other end contains exposed hydroxyl groups; the linker arm system of this invention uses phthalates or alkyl esters as the base-sensitive core structure, which can be cleaved under sodium methoxide conditions, and after hydrogenation deprotection, retains free anomeric sites at the ends of the polysaccharides, or provides amino and carboxyl groups for subsequent preparation of glycoconjugates and glycochips. During the cleavage of the linker arm, the ester protecting groups of the polysaccharide can be removed simultaneously, simplifying the deprotection step and improving efficiency and yield.

The invention relates to an octapeptide with ADH activation capability and a preparation method thereof, and belongs to the technical field of biology. The octapeptide is abbreviated as NDDDFIRI, the molecular weight of the octapeptide is 1007.20, and the sequence of the octapeptide is as follows: Asn-Asp-Asp-Asp-Phe-Ile-Arg-Ile; the method comprises the following steps: selecting macromolecular resin, according to the characteristics of an amino acid sequence Asn-Asp-Asp-Asp-Phe-Ile-Arg-Ile, connecting hydroxyl of Ile with the resin, then carrying out a shrinkage reaction and treatment on amino of Arg and carboxyl of Ile, then adding Ile, carrying out a reaction on amino of Ile and carboxyl of Arg, sequentially adding amino acids from right to left, adding the last Asn amino acid, and then cutting off the resin to obtain the target polypeptide. According to the invention, hemp seed protein is taken as a raw material, a biological enzymolysis technology is combined with bioinformatics and a molecular docking technology to screen octapeptide with ethanol dehydrogenase activation activity, and polypeptide synthesis and in-vitro activity determination are carried out through a solid-phase synthesis technology. The polypeptide with the hemp seed protein source capable of activating the activity of ethanol dehydrogenase is obtained and can be used for developing medicines with the functions of dispelling the effects of alcohol and protecting the liver.

The invention relates to a biotechnology, in particular to oligopeptide and application thereof in resisting multiple drug resistance of escherichia coli. The amino acid sequence of the oligopeptide (SZP) is shown as SEQ ID NO.1, and the homology of the oligopeptide (SZP) is more than 80%. The oligopeptide is an oligopeptide of a target AcrAB-TolC, and the amino acid sequence of the oligopeptide is SEQ ID NO. 1X1YX2RX3FVVX4X5; wherein X1 is selected from R, Y, H or K; x2 is selected from R, K or H; x3 is selected from G, F, Y, R, K or H; x4 is selected from G, A, W, F, D, E, K or H; and X5 is selected from G, D, E, R, K or H. The active peptide SZP disclosed by the invention can be used for remarkably enhancing the antibacterial activity of various antibiotics to multidrug-resistant escherichia coli through an efflux pump for generating multidrug resistance by targeting dominant bacteria, enhancing the permeability of cell membranes and a multidimensional mechanism for influencing the proton gradient of inner membranes of the bacteria, and can be obtained through a solid-phase synthesis technology, so that the preparation cost is relatively low.

This invention belongs to the field of solid-phase synthesis technology. A method for preparing aflatoxin lysine adduct based on solid-phase synthesis includes the following steps: (1) synthesis of an amino acid-supporting resin; (2) deprotection of the amino acid resin to obtain N-α-Boc-lysine resin; (3) cyclization to obtain N-ε-aflatoxin dialdehyde-N-α-Boc-lysine resin; (4) oxidation to obtain N-ε-aflatoxin-N-α-Boc-lysine resin; (5) cleavage and purification to obtain the aflatoxin lysine adduct. This invention provides an aflatoxin lysine adduct. This invention also provides a standard for the aflatoxin lysine adduct. This invention utilizes solid-phase synthesis technology to synthesize aflatoxin amino acid adducts on resins, especially the efficient synthesis of AFB1-Lys, providing reliable standards for clinical medical diagnosis and food testing. Particularly in the determination of serum albumin aflatoxin adducts, it greatly assists in the accurate monitoring of aflatoxin exposure levels.

The present invention discloses a solid phase synthesis method of flurana, which uses amino-protected glycine as a starting material, is connected to a solid phase resin to obtain resin 1, and then deamination protection is obtained to obtain resin 2; then solid phase reaction is carried out in sequence to obtain resin 3 and resin 4, and then a cutting liquid is added to separate the synthesized key structure from the solid phase resin to obtain a key intermediate F of flurana; the key intermediate F is condensed with 2,2,2-trifluoroethylamine to obtain flurana. The starting raw materials of this method are cheap and easy to obtain, and the technology of solid phase synthesis is applied. The process of synthesizing the key intermediate F saves tedious purification steps such as column chromatography or recrystallization. The method is novel, simple to operate, saves time, and has low yield loss, which meets the characteristics of an automated continuous production process. This method mainly relies on solid phase synthesis technology, can effectively improve product quality and yield, reduce operational difficulty, and enhance the continuity of the flurana synthesis process.

The present application relates to the field of biological medicine, and particularly relates to a polypeptide library with diverse structures, a construction method and application thereof. Each polypeptide in the polypeptide library has a general formula shown in formula I: Acp-K-X1C1X2X3X4C2X5X6X7C3X8X9X 10 C4E (I); wherein, X1-X 10 are any amino acid residues which can be randomized; K is lysine; C1-C4 are cysteine; and E is glutamic acid. Through solid-phase synthesis technology under mild conditions, the polypeptide intramolecular disulfide bond and amide bond pairing are precisely controlled, and rapid cyclization is performed, so that a polypeptide library with diverse structures is constructed. The synthesized linear peptides, cyclic peptides and polycyclic peptides are subjected to high-throughput screening against different cell models, and a target cell-penetrating peptide with selectivity for penetrating cell membranes is obtained, which provides a solid foundation for active polypeptide molecule discovery and development of polypeptide innovative drugs.