84 results about "Cysteine formation" patented technology

Provided are a glucagon-like peptide-1 (GLP-1) analogue monomer and dimmer, a preparation method thereof, and an application thereof. The GLP-1 analogue monomer comprises one cysteine; and the dimer is formed by two monomer molecules connected via an intermolecular disulfide bond formed by the cysteine. The GLP-1 monomer comprising cysteine has the following general formula: 7HAEX10TFTSX15VSSYLEX22X23AAKEFIX30WLX33KGRG37, wherein X10 is glycine or cysteine, X15 is aspartate or cysteine, X22 is glycine or cysteine, X23 is glutamine or cysteine, X30 is alanine or cysteine, and X33 is valine or cysteine; and only one of X10, X15, X22, X23, X30, and X33 is cysteine. The glucagon-like peptide-1 analogue dimer of the present invention has an in vivo half-life of more than 8 to 96 hours, thus facilitating clinical promotion and application.

The invention provides a GLP-1 dimer, a preparation method therefore and an application thereof. The GLP-1 dimer is formed by two GLP-1 monomers containing cysteine connected via a disulfide bond formed by cysteine. The general formula of the GLP-1 monomer containing cysteine is 7HAEX10T FTSX15V SSYLE X22X23AAKEFIX30W LX33KGR G37; wherein X10 is aglycine or cysteine, X15 is aspartic acid or cysteine, X22 is glycine or cysteine, X23 is leucine or cysteine, X30 is alanine or cysteine, X33 is valine or cysteine, and only one among X10, X15, X22, X23, X30 and X33 is cysteine. The GLP-1 dimer in the invention has an in vivo half-life of more than 8 to 96 hours, thus greatly facilitating clinical promotion and application.

The invention relates to application of scolopendra mutilans neurotoxin peptide omega-SLPTX-Ssmla, belonging to the field of biomedicine. A primary sequence of the omega-SLPTX-Ssmla comprises 83 amino acid residues, wherein three pairs of disulfide bonds are formed by six aminothiopropionic acids, and the molecular weight is 8811.3 Da. The code of the neurotoxin gene comprises 426 nucleotides of which include signal peptides, premise peptides and mature peptides. The scolopendra mutilans neurotoxin omega-SLPTX-Ssml has a quite obvious enhancement effect on calcium ion channel current on a dorsal ganglion root and is a novel calcium channel agonist. The scolopendra mutilans neurotoxin omega-SLPTX-Ssm provided by the invention can be used for increasing the openness of the calcium channel to enable calcium ions to flow internally and preparing medicaments for treating calcium channel diseases and can also be used as a new tool reagent for calcium channel researches.

The invention provides a group of peptides as well as a pharmaceutical composition and application thereof. The peptides are as shown in sequence tables; the peptides have amino acid sequences with an analgesic effect, or are pharmacologically acceptable salts of the peptides. A ring is formed by two cysteines at the head end and the tail end of each peptide. A pharmacophore (a structural domain) which has abirritation in the GsMTx-4 peptide is determined by comparing multiple inhibitor cystein knot (ICK)-containing peptide sequences such as GsMTx-4 and GsMTX-2 and carrying out behavior test on a rat pain model.

The invention relates to an anabaena PCC7120 fat oxygenase gene which belongs to the biologic technical field of the food industry. The gene is derived from anabaena sp. PCC7120 and is multiplied andobtained from genome DNA by PCR, colibacillus is converted after an expression vector is inserted and is induced to express, and the expressed recombinant enzyme catalyzes the oxidation of unsaturatedfatty acid to generate a fatty acid hydrogen overoxidation derivative with conjugated double bonds. The hydroperoxide is used as an unstable primary enzyme promoting product and can further generatea series of oxidation secondary reactions. In the improvement of the quality of flour, the hydroperoxide has an important application value in the following two aspects: (1) oxidizing cysteine with reducibility, forming a disulfide bond, applying to the improvement of the quality of the flour, enhancing the strength of gluten and replacing potassium bromate with a carcinogenic action; and (2) oxidizing pigments, applying to the bleaching of the flour and replacing benzoyl peroxide.

The invention relates to an Odorrana grahami immunomodulation peptide, gene and variant and the application in the pharmacy belonging to the biomedicine field. The Odorrana grahami immunomodulation peptide is a circular peptide with a molecular weight of 1791.12 D and a isoelectric point of 9.84. The whole sequence of the Odorrana grahami immunomodulation peptide is Thr Ser Arg Cys Tyr Ile Gly Tyr Arg Arg Lys Val Val Cys Ser (TSRCYIGYRRKVVCS), wherein the fourth cysteine and 14th cysteine form intramolecular disulfide bond. The code gene is composed of 307 nucleotides, wherein the code mature parts are from 141th to 186th nucleotide. The produced variant is produced by substituting the fourth amino acid in the original sequence of the Odorrana grahami immunomodulation peptide. The artificial synthetic Odorrana grahami immunomodulation peptide and variant thereof has a strong immunomodulation activity and tumor resistance activity and can be used for immunomodulation, tumor treatment and chemotherapeutics. The invention has the advantages such as simple sequence and convenient synthesis.

The present invention relates to rana grahami antibiotic peptide and its application, and belongs to the field of biomedicine. Rana grahami antibiotic peptide is one kind of cyclic polypeptide separated from the secretion of amphibian rana grahami, and has molecular weight of 1705.3 dalton, isoelectric point of 9.39, and primary structure of polypeptide sequence Leu Lys Gly Cys Trp The Lys Ser Ile Pro Pro Lys Pro Cys Phe(LKGCWTKSIPPKPCF) with cysteines in the 4-th and 14-th forming intramolecular disulfide bond. Its preparation process includes collecting secretion of ether stimulated rana grahami, centrifuging to eliminate precipitate, freeze drying, chromatographic separation in filtering gel column and separating purification in reverse high pressure liquid chromatogram. The rana grahami antibiotic peptide has powerful effect of inhibiting bacteria, fungi and viruses and no hemolytic activity, and may be used in preparing medicine for treating pathogenic microbe infection diseases.

The present disclosure relates to a symmetric bispecific antibody of the class IgG4 comprising two heavy chains which each comprise a variable domain, CH1 domain and a hinge region, wherein in each heavy chain: the cysteine in the CH1 domain which forms an inter-chain disulphide bond with a cysteine in a light chain is substituted with another amino acid; and optionally one or more of the amino acids positioned in the upper hinge region is substituted with cysteine, wherein the constant region sequence of each heavy chain is similar or identical and the variable region in each heavy chain is different, formulations comprising the same, the use of each of the above in treatment and processes for preparing said antibodies and formulations.

Disclosed is an pharmacy application of both a serine protease inhibitor of Rana grahami Graham's frog and a gene thereof, pertaining to biomedicine field. Serine protease inhibitor of Rana grahami Graham`s frog is a cyclic polypeptide encoded by a gene of Rana grahami Graham's frog, which is a Chinese amphibian. Said serine protease inhibitor has a molecular weight of 1951.38 dolton, an isoelectric point of 9.51, and no enzymatic activity. The complete sequence thereof is NH2-AVNIPFKVHFRCKAAFC-COOH,in which Cys at 12th site and Cys at 17th site form an intramolecularly disulfide bond. The coding gene is composed of 301 nucleotides, and the mature coding part is nucleotides from 160th site to 213th site. Artificial serine protease inhibitor of Rana grahami Graham's frog has strong suppression activity for serine protease, and can be used in pharmacy for preparing medicine for tumor, gastritis, and pancreatitis. Said serine protease inhibitor has a simple sequence and can be synthesized with ease.

The present invention discloses an amino terminal brain natriuretic peptide precursor polypeptide. The amino terminal brain natriuretic peptide precursor polypeptide is formed by respectively adding first cysteine and second cysteine near an amino terminal end and a carboxy terminal end of a specific amino acid sequence of a native amino terminal brain natriuretic peptide precursor. The first cysteine and the second cysteine are capable of forming a disulfide bond, the specific amino acid sequence is selected from one or more of the polypeptide sequences shown as SEQ ID NO. 1, and / or the specific amino acid sequence is selected from one or more of the polypeptide sequences shown as SEQ ID NO. 2, the vicinity of the amino terminal is 1 to 3 amino acids at the amino terminal of the specificamino acid sequence, and the vicinity of the carboxyl terminal is 1 to 3 amino acids at the carboxy terminal of the specific amino acid sequence. The invention also discloses an antibody and a preparation method thereof. The invention also discloses a detection kit. The invention also discloses a method for detecting the amino terminal brain natriuretic peptide precursor.

The invention relates to a stable CD3-CD19 resisting mini-type difunctional antibody of disulfide bond and a preparation method thereof. The preparation method comprises the steps of based on the CD3-CD19 resisting antibody, introducing amino acid Cys mutation in the CD3VL-resisting 100th amino acid Ser and CD3VH-resisting 44th amino acid Gly, wherein the expressed product has the structure of disulfide bond formed by the CD3VL-resisting 100th and the CD3VH-resisting 44th cysteines shown in the sequences 3 and 4. The stable CD3-CD19 resisting mini-type difunctional antibody of disulfide bond introduces cysteine mutation in the bits of VL-100 and VH-44 in the CD3-resisting variable region, and the disulfide bond is formed in a bacterium periplasm cavity between the variable region fragments of the two expressed single chains, i.e., between the CD3VL-CD19VH resisting segment and the CD19VL-CD3VH resisting segment, thereby enhancing the stability of the antibody; besides, a mutational site is located in a conservative framework region and two mutational sites in the space conformation are closer enough without generating tension so that the activity of the transformed difunctional antibody remains unchanged and the stability is enhanced.

The invention discloses a staphylokinase mutant, wherein cysteine is introduced to the C-end of the staphylokinase mutant. Compared with the wild type staphylokinase, the C-end of the mutant has three more amino acids, namely glycine-glycine-cysteine (Gly-Gly-Cys). The invention also discloses a preparation method of the dimer of the staphylokinase mutant. The dimerization method of the staphylokinase is that the two maleimide groups of the homotype bifunctional binder 1,4-dimaleimide butane and the cysteine at the C-end of the staphylokinase are utilized to form a stable covalent bond. The invention also discloses a preparation method for realizing the N-end site-specific modificaton of polyethylene glycol by using the dimer of the staphylokinase mutant. Under special conditions, methoxy polyethylene glycol-propionaldehyde is connected with one N-end of the staphylokinase dimer molecule through the covalent bond. The biological activity of the polyethylene glycol modified product of the staphylokinase dimer is higher than that of the modified product of the staphylokinase monomer.

The invention relates to an amino acid sequence and a gene sequence of cyriopagopus albostriatus toxin mu-TRTX-Ca1a, and application, and belongs to the field of biomedicine. The mu-TRTX-Ca1a contains38 amino acid residues, wherein six cysteines form three pairs of disulfide bonds, and the molecular weight is 4289.31 Da. The cyriopagopus albostriatus toxin mu-TRTX-Ca1a can preferentially inhibitsodium channel subtype Nav1.7. The cyriopagopus albostriatus toxin mu-TRTX-Ca1a can remarkably alleviate the pain caused by a mice formalin model, an acetic acid writhing model and a hot plate model,and can be used as a drug for treating pain.

The invention discloses a nanorana alpine antioxidative peptide and application thereof. The antioxidative peptide is a cyclic peptide composed of 29 amino acids, the amino acid sequence of the antioxidative peptide is as shown in SEQ ID NO.1, and cysteine at the seventh position and cysteine at the twelfth position form an intramolecular disulfide bond. The invention further discloses nucleotide for coding the antioxidative peptide of the nanorana pleskei. The antioxidative peptide has good anti-inflammatory and anti-oxidation effects, can protect plasmid DNA damaged by H2O2, inhibits accumulation of CuSO4 induced zebrafish larva active oxygen and migration of neutrophil, and relieves mouse skin injury induced by UVB radiation.

The invention provides application of a molecular allosteric body and dimer of a human growth hormone releasing hormone (hGHRH) similar peptide in treating GH deficiency, infertility, senile dementiaand diabetes and enhancing immunity. The dimer is formed by connecting two identical hGHRH similar peptide monomers containing a single cysteine molecule allosteric structure through a disulfide bondformed by cysteine, and an H-shaped structure (intramolecular single Ser-to-Cys substitution) is formed. A side chain epsilon-amino of one lysine of the GHRH similar peptide is also subjected to fattyacid chain modification. Through fatty acid modification, the GH sustained release time of the GHRH similar peptide monomer or dimer is prolonged in vivo, and the longest release time reaches 17 days. The invention finds that the GHRH dimer with long-acting activity has an Aib-to-2Ala substitution structure, an 18C-to-18C disulfide bond formation structure, a C20 fatty acid chain modification structure and a C-terminal amidation structure.

A method for selectively protecting restriction enzyme cutting sites in a trypsin digestion process is characterized in that a polypeptide to be digested by trypsin is prepared, cysteines are arrangedon the two sides of arginine of the polypeptide, two cysteines form a disulfide bond, and the disulfide bond stretches across arginine. Appropriate sites are selected to insert cysteine or unimportant amino acids are mutated into cysteine on two sides of arginine needing to be protected in polypeptide, and two cysteines stretch over arginine to be protected to form a disulfide bond. Through the conformation change caused by the disulfide bond, steric hindrance is formed at the enzyme cutting sites, the affinity of trypsin and arginine carboxyl terminals is reduced, and the enzyme digestion effect is greatly weakened or even eliminated.

The invention relates to the technical field of protein engineering, in particular to an alginate lyase mutant with high catalytic activity and application thereof. The alginate lyase mutant is obtained by mutation of any one or more sites of cysteine at the 82<nd> site, cysteine at the 95 site, aspartic acid at the 146 site, cysteine at the 209 site and amino acids forming hydrogen bonds with the cysteine at the 82<nd> site, the 95 site or the 209 site of alginate lyase AlgAT5. The alginate lyase mutant or the expression microorganism of the alginate lyase mutant can catalyze algin to be subjected to beta elimination reaction to prepare alginate oligosaccharide, so that the catalysis efficiency of algin lyase is remarkably improved, the reaction time is shortened, and industrial development and application of the algin lyase are accelerated.

The invention discloses a method for improving moso bamboo cellulase hydrolysis conversion efficiency through amino acid-based deep eutectic solvent pretreatment, and belongs to the technical field of biomass recycling. The method comprises the following steps: mixing an L-cysteine solid and a formic acid solution, performing water bath heating to prepare an acidic eutectic solvent, performing microwave-assisted eutectic solvent pretreatment on moso bamboos, and performing filtration separation and enzymolysis; wherein the molar ratio of the L-cysteine to the formic acid is 1: (4-5). A deep eutectic solvent formed by formic acid and cysteine has a strong hydrogen bond network and an acid environment, beta-O-4 ether bonds in lignin are promoted to be broken, sulfydryl of cysteine participates in nucleophilic attack, a lignin-carbohydrate complex is further destroyed, formic acid can hydrolyze acetyl and glucosidic bonds in hemicellulose, and the lignin-carbohydrate complex is further destroyed. And degrading into an oligomer or monosaccharide. The phyllostachys pubescens components are efficiently separated, the cellulose enzymolysis saccharification capacity is improved, and effective utilization of all the phyllostachys pubescens components is facilitated.

The invention relates to an active polypeptide and its gene and an application of the inhibition peptide in pharmacy. The hoplobatrachus rugulosus proteinase inhibition peptide is cyclopeptide composed of 33 amino acids, a molecular weight is 3768.33 dalton, the isoelectric point is 6.303, and an amino acid sequence is SEQ ID NO.1, and a third cysteine and an eighth cysteine of the polypeptide form intramolecular disulfide bond. A gene sequence of the hoplobatrachus rugulosus proteinase inhibition peptide is composed of SEQ ID NO.4, wherein, the matured hoplobatrachus rugulosus proteinase inhibition peptide is 379th-477th site nucleotide. The hoplobatrachus rugulosus proteinase inhibition peptide has the characteristics of simple structure, convenient artificial synthesis, wide antibacterial spectrum, and strong activity. and can be taken as a medicine for treating pathogenic microorganism infectious diseases and a medicine having functions of beauty treatment and skin caring.

The invention relates to a hydroxyethyl starch modified hemopoietin mimic peptide with a long-acting erythropoiesis promoting function and a medicinal salt thereof. The invention further provides a preparation method for the hydroxyethyl starch modified hemopoietin mimic peptide and use thereof in preparing drugs for treating diseases which are characterized by being short of erythrocyte and erythrogenin or being short of erythrocyte groups or being in defect of erythrocyte groups. The hydroxyethyl starch modified hemopoietin mimic peptide provided by the invention is represented by a formula I as shown in the description, wherein two cysteines form a disulfide bond, X represents succinic hydroxyethyl starch, C represents a lysine at a tail end, and (K) is condensed with carboxyl of X through free amino of a side chain.

The invention relates to an erythropoietin mimetic peptide derivative having a long-acting erythropoiesis function and a medicinal salt thereof. The invention also provides a preparation method of the erythropoietin mimetic peptide derivative, and a use of the erythropoietin mimetic peptide derivative in the preparation of medicines for treating diseases characterized by lacking of erythropoietin or erythrocyte population deficiency or defect. The erythropoietin mimetic peptide derivative is a polypeptide represented by SEQ ID NO:1 GGLYACHMGPITNalVCQPLRSarKVPGPGVPGPGVPGPGVPGPG, wherein two cysteines of the polypeptide form a disulfide bond, and the N end is acetylated.

The invention discloses a staphylokinase mutant, wherein cysteine is introduced to the C-end of the staphylokinase mutant. Compared with the wild type staphylokinase, the C-end of the mutant has three more amino acids, namely glycine-glycine-cysteine (Gly-Gly-Cys). The invention also discloses a preparation method of the dimer of the staphylokinase mutant. The dimerization method of the staphylokinase is that the two maleimide groups of the homotype bifunctional binder 1,4-dimaleimide butane and the cysteine at the C-end of the staphylokinase are utilized to form a stable covalent bond. The invention also discloses a preparation method for realizing the N-end site-specific modificaton of polyethylene glycol by using the dimer of the staphylokinase mutant. Under special conditions, methoxypolyethylene glycol-propionaldehyde is connected with one N-end of the staphylokinase dimer molecule through the covalent bond. The biological activity of the polyethylene glycol modified product of the staphylokinase dimer is higher than that of the modified product of the staphylokinase monomer.

The invention discloses an artificial synthetic antibacterial peptide with a beta-hairpin structure. The amino acid sequence is as follows: Cys-Ile-Cys-Arg-Arg-Gly-Phe-Cys-Val-Cys. Two arginines existin the corner position of the antibacterial peptide to form active sites where positive charges are concentrated; at the same time, a glycine exist in the corner position, so that the formation and stability of the corner structure are improved; four cysteines exist in the two arm positions to form two pairs of disulfide bonds; at the same time, hydrophobic amino acids exist in the two arm positions, so that the hydrophobicity of two arms is enhanced, and the insertion of the two arms into a bacterial cell membrane is facilitated; and the amidation design exist at the sequence C-terminus, sothat the charge influences at two ends of the sequence are reduced. Experiments show that the above antibacterial peptide provided by the invention can effectively inhibit or even kill staphylococcusaureus, escherichia coli, and aerobic spore bacteria, and has a good inhibitory effect on most of gram-positive bacteria.

The invention relates to erythropoietin mimic peptide. The erythropoietin mimic peptide is characterized in that the amino acid sequence of monomer peptide of the mimic peptide is shown as GX1LYACHMGPITX2VCQPLRX3K in SEQ ID NO:1, wherein X1 is allylglycine (D-Allyiglycin), X2 is 3-(1-naphthyl)-L-alanine (Nal), X3 is sarcosine (Sar), 6-bit and 15-bit cysteine (C) forms an intramolecular disulfide bond, and N is acetylized in end. The invention further provides a preparation method of the mimic peptide, a preparation method of dimer and pharmaceutical salt of the mimic peptide. The invention further provides a pharmaceutical composition containing the mimic peptide or the dimer or the pharmaceutical salt of the mimic peptide. The erythropoietin mimic peptide, the dimer and the pharmaceutical salt of the mimic peptide can excite generation of erythrocyte and significantly prolong the half-life period of drugs in human bodies.

The invention relates to a hmopoietin mimic peptide with long-acting erythropoiesis-promoting function and pharmaceutical salts. The invention also provides a preparation method for the above mopoietin mimic peptide and application of the mopoietin mimic peptide to prepare medicines treating diseases with the character of erythrocyte lack, erythropoietin lack, or erythrocyte population lack or defect. The provided hemopoietin mimic peptide is an alkyl acid conjugate of a lysine (K) side-chain dissociated amino at the terminal of a peptide chain shown as SEQ ID NO:1, the structural general formula is shown as a formula I: GGLYACHMGPITNalVCQPLRSarK-X, wherein two cysteine form a disulfide bond, the N terminal is acylated, and X represents lauric acid or palmitic acid.

The invention provides the molecular degeneration of human growth hormone release hormone (HGHRH) peptides and its di clustering in the treatment of GH deficiency, infertility, dementia, diabetes, and enhanced immunity.The di agent of the present invention is two similar HGHRH -like peptide monomers that contain a single beurine molecular degeneration are connected by a sulfur (sulfurine formed by cysteine, and form an H -shaped structure (internal single ser → CYS inside the molecule → CYSreplace).The present invention also modifies the fatty acid chain of one of the lysine ε‑ amino groups of one of the lysine in the GHRH -like peptide.Extend the GHRH -like peptide monomer or di -polycatus in the body through fatty acid decoration, up to 17 days in the GH in the body.The present invention found that GHRH diodes with long -term activity have AIB → 2 ALA replacement, 18 C‑ 18 C formal sulfur formation, C20 fatty acid chain modification, and C -side amineization structure.

The invention relates to the technical field of protein engineering, in particular to a mutant of alginate lyase with high catalytic activity and its application. The mutants are cysteine ​​at position 82, cysteine ​​at position 95, aspartic acid at position 146, cysteine ​​at position 209, and cysteine ​​at position 82, 95 or 209 of alginate lyase AlgAT5 Any one or several positions of amino acids that form hydrogen bonds with amino acids are mutated. The mutant of the present invention or the microorganism expressing it can catalyze the β-elimination reaction of alginate to prepare alginate oligosaccharides. This method significantly improves the catalytic efficiency of the alginate lyase, reduces the reaction time, and helps to accelerate the industrial development and application of the alginate lyase.

The invention provides a melittin polymer, which is formed by at least connecting disulfide bonds between two melittin variant molecules after a melittin variant is formed by mutating alanine at the fourth site of an amino acid sequence of a melittin monomer into cysteine and mutating isoleucine at the twentieth site into cysteine in the amino acid sequence of the melittin monomer. The preparation method of the melittin polymer comprises the following steps: obtaining a melittin variant through escherichia coli recombinant expression, and purifying and oxidizing the obtained melittin variant through a nickel column to obtain the melittin polymer, and carrying out gel filtration chromatography on the obtained melittin polymer to obtain the purified melittin polymer. The invention also provides an application of the melittin polymer, and the melittin polymer is used for preparing antibacterial drugs or antibacterial feed additives. The prepared melittin polymer can effectively reduce the toxicity to red blood cells, has relatively strong environmental responsiveness and stability, and can effectively prolong the antibacterial aging.

The invention discloses a tree frog antibacterial peptide as well as a gene and application thereof. The tree frog antibacterial peptide provided by the invention is a cyclic peptide consisting of 29 amino acids, the amino acid sequence of the tree frog antibacterial peptide is shown as SEQ ID NO.1, and the third cysteine and the seventh cysteine form an intramolecular disulfide bond. The invention also provides a nucleotide sequence for coding the tree frog antibacterial peptide, wherein the nucleotide sequence is shown as SEQ ID NO.2 or SEQ ID NO.9. The invention also provides a nucleotide sequence for coding the tree frog antibacterial peptide. The tree frog antibacterial peptide disclosed by the invention has very strong treatment functions of antibiosis, anti-inflammation, antioxidation and immunoregulation, has the characteristics of simple structure and convenience in artificial synthesis, and can be used for preparing medicines for treating pathogenic microorganism infection, autoimmune diseases and even sepsis.

The invention belongs to the technical field of polypeptide preparation, and particularly relates to a bamboo shoot conus polypeptide Te-SS II and application thereof in analgesia. The conus polypeptide toxin Te-SS I with analgesic activity is found from bamboo shoot conus by utilizing high-throughput transcriptomics, then linear peptide is synthesized by adopting a polypeptide solid-phase synthesis method, an oxidized peptide Te-SS II containing one disulfide bond is obtained after the disulfide bond is formed by adopting an air oxidation method, then the oxidized peptide Te-SS II is purified by adopting high performance liquid chromatography, and mass spectrum identification is performed. The Te-SS II has one disulfide bond formed by two cysteines and has an efficient analgesic effect on zebra fish and mice. Therefore, the bamboo shoot conus polypeptide Te-SS II provided by the invention can be used for preparing analgesic products, and a new breakthrough is brought to the field of pain treatment.