33 results about "Peptide Synthesis technique" patented technology

The invention provides a solid-liquid combined synthesis method of semeglutide, which belongs to the technical field of semeglutide synthesis, and specifically comprises the following steps: segmenting a main chain of the semeglutide into three shorter polypeptide fragments, namely a fragment 4, a fragment 5 and a fragment 2 at sites 7-14, 15-22 and 23-37, and respectively synthesizing at the same time; performing solid-phase assembly on the fragment 4 and the fragment 5 to form 7-22 peptide fragments, namely a fragment 1, and after the fragment 1 is cut off from the resin, forming NHS ester at a C end; after the fragment 2 is assembled, selectively removing a protecting group A11oc on the Lys26, then connecting with a side chain for fatty acid treatment to form a fragment 3, and cutting off the fragment 3 from the resin; and connecting the NHS ester of the fragment 1 with the fragment 3 in a liquid phase reaction system. The crude semeglutide prepared by the synthetic method is relatively high in yield and purity. The refined semeglutide of which the purity is more than 99.3% and the content of single impurity is less than 0.1% can be obtained at high yield through a conventional purification means.

The invention provides a preparation method of tiall peptide, and belongs to the technical field of polypeptide synthesis, according to the preparation method, a small amount of lysis solution is adopted for lysis, a small amount of poor solution composed of methyl tert-butyl ether and n-heptane with the volume ratio of 1-2: 1 is used for crude peptide precipitation, precipitated particles are uniform, large and not prone to caking, the crude peptide impurity level is lower, and the purity of the crude peptide is higher. The method has the advantages that the method is simple in process and easy in subsequent purification step, the amount of generated waste liquid is small, the activating agent 7-(1H-pyrrolo [2, 3-b] pyridine-1-yl)-1H-benzo [d] [1, 2, 3] triazole-1-alcohol is used for activating amino acid, the coupling reaction degree is high, and the target peptide yield is high. The preparation method of the tilpotide has the advantages of being simple, economical, capable of achieving mass production, low in impurity content, high in purification yield, high in yield and the like.

The invention relates to the technical field of polypeptide synthesis, in particular to a synthetic method of desmopressin acetate. The synthesis method of the desmopressin acetate comprises the following steps that Fmoc-protected amino acids are coupled on amino resin one by one according to the sequence of the desmopressin acetate to obtain peptide resin, and the Fmoc-protected amino acids comprise Fmoc-Gly-OH, Fmoc-D-Arg (Pbf)-OH, Fmoc-Pro-OH, Fmoc-Cys (Trt)-OH, Fmoc-Asn (Trt)-OH, Fmoc-Gln (Trt)-OH, Fmoc-Phe-OH, Fmoc-Tyr-OH and Mpa (Trt)-OH; and carrying out cracking, oxidation, purification and salt conversion on the peptide resin to obtain desmopressin acetate. According to the synthesis method disclosed by the invention, Fmoc-protected amino acid without side chain protection is adopted, so that the generation of a specific impurity Mpa (tBu)-Tyr-Ph-Gln-Asn-Cys-Pro-D-Arg-Gly-NH2 can be effectively prevented, and the purity and the yield of the product are effectively improved.

The invention discloses a production process of melittin, belongs to the technical field of polypeptide synthesis, and particularly relates to a preparation method of melittin, which comprises the following steps: synthesizing melittin-peptide resin by adopting a solid-phase synthesis method according to the sequence of melittin sequences, and cutting and purifying to obtain melittin; in the solid-phase synthesis method, amino acid reagents are coupled one by one or at least more than one melittin peptide fragment and a single amino acid reagent are adopted for coupling, and the number of amino acids in the melittin peptide fragment is 4-8. The melittin peptide fragment is synthesized by adopting a liquid-phase synthesis carrier, and the liquid-phase synthesis carrier is obtained by synthesizing 2, 4-dihydroxy benzaldehyde, 1, 4-dibromocyclohexane and diethyl bromomalonate and reducing the 2, 4-dihydroxy benzaldehyde, the 1, 4-dibromocyclohexane and the diethyl bromomalonate.

The application relates to the technical field of peptide synthesis, and discloses a preparation method of a snake venom-like tripeptide, which comprises the following steps: condensing Boc-beta-Ala-OH and H-Pro-OMe, hydrolyzing the methyl ester groups to obtain Boc-beta-Ala-Pro-OH; condensing Boc-Gln-OH and benzylamine, and removing Boc to obtain H-Gln-NHBzl; then condensing Boc-beta-Ala-Pro-OH and H-Gln-NHBzl to prepare a polypeptide; and after the Gln in the polypeptide is subjected to Hofmann rearrangement, the Boc protection group in the polypeptide is removed to obtain the snake venom-like tripeptide. The preparation method adopts liquid-phase synthesis of the snake venom-like tripeptide, the synthesis route is short, the reaction condition is mild, special equipment and reagents are not needed, the operation steps are simplified, the process cost is reduced; the reaction reagents used are cheap and easy-to-obtain industrial reagents, the raw material cost is reduced; and the product purity can reach more than 99%.

The utility model discloses an infinitely coupled polypeptide synthesis device, which relates to the technical field of polypeptide synthesis and comprises a mounting table and a rotary mixing device, a servo motor is fixedly mounted at the top of the mounting table, and the output end of the servo motor is fixedly connected with a rotating shaft; the rotary mixing device comprises a polypeptide synthesis tank, a stirring rod, a bevel gear, an arc-shaped connecting plate, a circular ring and a bevel gear ring, the polypeptide synthesis tank is fixedly connected to the front end of the rotating shaft, the stirring rod is rotationally connected to the interior of the polypeptide synthesis tank, and the right end of the stirring rod extends to the exterior of the polypeptide synthesis tank and is fixedly connected with the bevel gear; the amino acid raw materials roll up and down and left and right in the polypeptide synthesis tank through rotation of the polypeptide synthesis tank, the amino acid raw materials with large density and the amino acid raw materials with small density are prevented from being separated from each other, the phenomenon that the amino acid raw materials are layered is avoided, and mixed reaction and infinite coupling of different amino acid molecules are better facilitated.

The invention relates to isolated polypeptide targeting MPP8 protein and application of the isolated polypeptide, and belongs to the technical field of biological medicine. According to the scheme, a bifunctional molecule with high affinity is formed by utilizing a small molecule chip synthesis technology and a solid phase polypeptide synthesis technology and combining an azide-alkyne cycloaddition reaction, and the affinity and functions of the bifunctional molecule are comprehensively verified through methods such as SPR, Western blot and cell proliferation. Compared with an existing technical scheme, the method has the advantages that the synthesis cost is reduced, the reaction speed is increased, the reliability of quality control and function verification is enhanced, the stability and consistency of the compound are ensured, and the method is suitable for large-scale production and application and has a wide market application scene.

The application discloses a semi-chemical synthesis method of an N-terminal domain of matrix metalloproteinase inhibitor-2 (N-TIMP2) and application thereof. The N-TIMP2 is divided into three fragments, wherein a key tyrosine post-translational modification site is located in the fragment 2; the polypeptide resins of the fragment 1 and the fragment 2 are synthesized by using a solid-phase polypeptide synthesis technology, and the fragment 1 and the fragment 2 with a C-terminal hydrazide are obtained after cleavage, deprotection, extraction and purification; the fragment 3 is obtained by combining an E. coli recombinant expression technology and a three-step one-pot selective protection reaction of side chains of mercapto; the fragment 1, 2 connecting product is obtained through a first-step natural chemical connecting reaction; the full-length linear protein is obtained through a second-step natural chemical connecting reaction, desulfurization and deprotection; and finally, the N-TIMP2 protein is obtained through a refolding reaction. The semi-chemically synthesized N-TIMP2 protein has a comparable MMP-14 inhibiting activity to the N-TIMP2 protein obtained by using the E. coli recombinant expression technology.

The invention provides a preparation method of polypeptide containing Sar linker, and belongs to the technical field of polypeptide synthesis. The preparation method of the polypeptide containing the Sar linker comprises the following steps: (1) carrying out condensation reaction on Fmoc-beta-Asp-PG-(Sar) m-OH and H-Sar-OH, so as to obtain Fmoc-beta-Asp-PG-(Sar) n-OH; and (2) carrying out deprotection treatment on the Fmoc-beta-Asp-PG-(Sar) n-OtBu, so as to obtain the Fmoc-beta-Asp-(Sar) n-OH. The polypeptide containing the Sar linker is prepared by adopting a full liquid phase synthesis method under mild conditions, the product yield is stable, the purity is high, and the post-treatment method is simple, so that the method is beneficial to industrial large-scale production.

The invention discloses a solid-phase synthesis method of Mortudotide, belongs to the technical field of polypeptide synthesis, and particularly relates to a method for synthesizing Mortudotide full-protection peptide resin by adopting a solid-phase synthesis method, then treating the Mortudotide full-protection peptide resin by adopting a cracking reagent to prepare crude Mortudotide. According to the present invention, during the chromatographic purification of the Macerdotide crude product peptide, the chromatographic column can be adopted to obtain the Macerdotide pure product peptide, the trithioacetone can be added to the cracking reagent, and the yield and the purity of the Macerdotide can be improved by using the trithioacetone. The solid-phase synthesis method of Macervide has the advantages of high yield, high purity, reduction of [-Tyr] and [-Thr] deletion impurities, and reduction of [+ Gly] increase impurities.

The invention provides a solid-phase synthesis method of tilpotitide, and belongs to the technical field of polypeptide synthesizing.According to the preparation method, a small amount of lysate is adopted for lysing, a small amount of poor solution composed of methyl tert-butyl ether and n-heptane with the volume ratio of 1-2: 1 is used for crude peptide precipitation, precipitated particles are uniform and large and are not prone to caking, and the solid-phase synthesis method is suitable for industrial production. Compared with the prior art, the method has the advantages that the crude peptide impurity level is lower, the subsequent purification step is easy, the amount of generated waste liquid is small, the activating agent 7-(1H-pyrrolo [2, 3-b] pyridine-1-yl)-1H-benzo [d] [1, 2, 3] triazole-1-alcohol is used for activating amino acid, the coupling reaction degree is high, and the target peptide yield is high. The solid-phase synthesis method of the tilpotide has the advantages of being simple, economical, capable of achieving mass production, low in impurity content, high in purification yield, high in yield and the like.

Relates to the field of solid-phase peptide synthesis technology, featuring the preparation and application of the specially designed RMBL resins. Structure of the RMBL resins is presented as Formaula (I). RMBL resin, a series of recyclable intramolecular acyl transfer linker loaded resin, can improve condensation efficiency of amino acids through an intramolecular acyl transfer mechanism, thus allowing efficient syntheses of common peptides, sterically hindered peptides, natural products of sterically hindered amino acid(s)-containing cyclic peptides, and their derivatives. The RMBL strategy developed facilitates efficient peptide synthesis under mild conditions, without additional activating reagents engaged, which meets the requirements of green chemistry. The RMBL strategy is the first-ever developed solid-phase peptide synthesis strategy taking advantage of the intramolecular acyl transfer mechanism, which enables optimized synthesis of sterically hindered peptides in a new reaction manner.

The present invention provides a method for preparing a polypeptide containing a Sar linker, which belongs to the technical field of polypeptide synthesis. The method for preparing a polypeptide containing a Sar linker comprises: (1) Fmoc- β ‑Asp‑PG‑(Sar) m ‑OH and H‑Sar‑OH undergo condensation reaction to obtain Fmoc‑ β ‑Asp‑PG‑(Sar) n ‑OH; (2) Fmoc‑ β ‑Asp‑PG‑(Sar) n ‑OtBu was deprotected to obtain Fmoc‑ β ‑Asp‑(Sar) n The present invention adopts a full liquid phase synthesis method to prepare a polypeptide containing a Sar linker under mild conditions. The product has a stable yield and high purity, and the post-processing method is simple, which is conducive to industrial scale-up production.

The invention discloses a preparation method of Fmoc-His, and relates to the technical field of polypeptide synthesis. Comprising the following steps: Fmoc-His (Trt) is taken as a raw material, trifluoroacetic acid is added, in addition, a proper amount of a catalyst is added to catalyze and remove a side chain protecting group to obtain a target product, the route mode avoids side reaction of main chain amino protection, avoids by-products of histidine under strong conditions, and simplifies the refining process; the method is cheap in initial raw material, simple to operate and suitable for industrial production, the yield is 85% or above, and the quality is stable. The compounds involved in the invention comprise amino acids containing side chain amino configurations, such as glutamine, asparagine, lysine, ornithine, cysteine, histidine, 2, 4-diaminobutyric acid, tryptophan and the like. The protective reagents involved in the invention comprise Mtt-cl, Cbz-Osu, MMt-Cl, Fmoc-OSU, (Boc) 2O and the like.

The invention discloses a preparation method of amino acid capable of protecting tetrapeptide, and relates to the technical field of polypeptide synthesis. The amino acid is Boc-Gly-Gly-Phe-Gly-OH, and the preparation method comprises the following steps: dissolving Boc-Phe-Gly-OH in N, N-dimethylformamide, then dropwise adding dimethyl sulfate under base catalysis, and then removing BOC protection in an HCl / ethyl acetate solution; the preparation method comprises the following steps: dissolving Boc-Gly-Gly-OH in dichloromethane, quickly dropwise adding a dichloromethane solution of oxalyl chloride in a reflux state, and reacting for a period of time after dropwise adding to obtain a Boc-Gly-Gly-Cl acyl chloride product; dissolving Phe-Gly-OMe-HCl in dichloromethane, dropwise adding triethylamine as an acid-binding agent, cooling with ice water, and dropwise adding the Boc-Gly-Gly-Cl acyl chloride product for reaction; and after treatment, dissolving the obtained solution in a mixed solution of tetrahydrofuran and methanol, carrying out saponification with liquid caustic soda, and carrying out treatment to obtain Boc-Gly-Gly-Phe-Gly-OH. Compared with the traditional reaction, the method does not need to use Pd / H2 to remove protection, and is safer. The acyl chloride intermediate does not need to be treated, so that the reaction is simpler and more efficient, and the reaction yield is favorably improved.

The invention discloses a preparation method of an amino acid derivative with a protected main chain carboxyl group, and relates to the technical field of polypeptide synthesis. Comprising the following steps: dissolving benzyl alcohol in anhydrous dichloromethane, adding amino acid until the system is turbid at the moment, and dropwise adding trimethylchlorosilane; according to the route, benzyl alcohol is protected by trimethylsilane to generate trimethylsilyl ester, the trimethylsilyl ester is active and is subjected to transesterification with amino acid, and meanwhile, HCl generated by the trimethylsilane and the benzyl alcohol and generated amino acid benzyl ester form hydrochloride. Compared with a traditional esterification reaction, trimethylchlorosilane is used as an HCl donor, environmental hazard is reduced, trimethylchlorosilane and benzyl alcohol can form trimethylsilyl ester, benzyl alcohol is activated in a phase change mode, the reaction rate is increased, the reaction yield is increased, and the method is suitable for industrial production. The invention relates to all common amino acids except tryptophan, serine and other amino acids containing side chain alcoholic hydroxyl groups and aspartic acid, glutamic acid and other amino acids containing side face carboxyl groups.

The utility model relates to the technical field of polypeptide synthesis, and discloses an efficient solid-phase polypeptide synthesis device which comprises a synthesis barrel, a barrel cover is arranged at the top of the synthesis barrel, barrel legs are arranged at the bottom of the synthesis barrel, a transverse plate is fixedly connected to the left side of the synthesis barrel, and stabilizing legs are fixedly connected to the bottom of the transverse plate. An adjusting column is fixedly connected to the top of the transverse plate, a first motor is fixedly connected to the top of the adjusting column, a lifting groove is formed in the right side of the adjusting column, a lead screw is arranged in the lifting groove, and a lifting block is in threaded connection with the surface of the lead screw. According to the efficient solid-phase polypeptide synthesis device, when the lead screw rotates, the lifting block can move up and down along the lead screw, the right side of the lifting block is fixedly connected with the barrel cover, and when the first motor drives the lead screw to rotate, the barrel cover can move up and down, so that the barrel cover can be conveniently opened and closed; and cleaning of the interior of the synthesis barrel is facilitated, manual opening of the barrel cover is avoided, and the manual labor amount is reduced.

The present invention discloses a solid-phase synthesis method of linaclotide, belonging to the technical field of peptide synthesis; the method adopts a solid-phase synthesis method, uses Fmoc-Tyr(tBu)-Wang resin as a starting material, and sequentially couples amino acids from the C-terminus to the N-terminus to obtain linaclotide peptide resin; then, after deprotection treatment, oxidation and cleavage, and purification treatment, linaclotide is obtained. The peptide sequence of linaclotide is as follows: H2N-Cys 1 ‑Cys 2 ‑Glu 3 ‑Tyr 4 ‑Cys 5 ‑Cys 6 ‑Asn 7 ‑Pro 8 ‑Ala 9 ‑Cys 10 ‑Thr 11 ‑Gly 12 ‑Cys 13 ‑Tyr 14 ‑OH (disulfide bridge: Cys 1 ‑Cys 6 &Cys 2 ‑Cys 10 &Cys 5 ‑Cys 13 The total yield of the linaclotide synthesized by the present invention is over 98%, and the purity is over 80.5%.

The invention discloses a solid-phase synthesis method of linaclotide, and belongs to the technical field of polypeptide synthesis. According to the method, a solid-phase synthesis method is adopted, Fmoc-Tyr (tBu)-king resin is taken as an initial raw material, amino acids are sequentially coupled according to the sequence from the C terminal to the N terminal, and linaclotide peptide resin is obtained; and carrying out deprotection treatment, oxidation, cracking and purification treatment to obtain linaclotide. The peptide sequence of the linaclotide is as follows: H2N-Cys1-Cys2-Glu3-Tyr4-Cys5-Cys6-Asn7-Pro8-Ala9-Cys10-Thr11-Gly12-Cys13-Tyr14-OH (a disulfide bond bridge: Cys1-Cys6amp, Cys2-Cys10amp, and Cys5-Cys13), and the peptide sequence of the linaclotide is as follows: the peptide sequence of the linaclotide is as follows: H2N-Cys1-Cys2-Glu3-Tyr4-Cys5-Cys6amp, Cys2-Cys10amp, Cys5-Cys13). The total yield of the synthesized linaclotide reaches 98% or above, and the purity of the linaclotide reaches 80.5% or above.

The utility model relates to the technical field of polypeptide synthesis, in particular to a polypeptide cracking reactor which comprises a reaction tank body and a filtering device, and a discharging opening is formed in the lower portion of the reaction tank body; the filtering device comprises a shell, a rotating mechanism, a feeding hole, a liquid outlet and at least two filtering barrels; the feeding hole is formed in the top surface of the shell and is connected with the discharging hole; the rotating mechanism is inserted into the filtering device from the upper part; the filtering barrel is arranged on the rotating mechanism and can rotate to the position below the feeding opening through the rotating mechanism. After the cracking reaction is completed, all materials are put into the filtering device through the discharging port to be filtered, filtrate is pumped out from the liquid outlet, filter residues are left in the filtering barrel, and by arranging the rotating mechanism, a new filtering barrel can be automatically switched to the position below the feeding port after one-time filtering for next-round filtering, so that the frequency of cleaning the filter residues by workers is reduced. And the reaction tank body can continuously work, so that the production efficiency is effectively improved.

The invention discloses a preparation method of an amino acid derivative containing side chain amino protection, and relates to the technical field of polypeptide synthesis. The preparation method comprises the following steps: dissolving Boc-His in a THF solution, adding alkali to adjust the pH value to be alkaline, adding Ts-Cl in batches at low temperature, and detecting the reaction progress through TCL until the reaction solution becomes clear; and carrying out extraction, concentration, recrystallization, stirring washing and drying on the reaction liquid to finally obtain the product Boc-His (Ts). The preparation method is few in side reaction, high in yield and low in raw polypeptide synthesis production cost, the mixing proportion of Boc-His, K2CO3 and Ts-Cl is equal in molar weight, the equal molar ratio can ensure the completeness of the reaction, reaction interruption caused by insufficient alkali is avoided, the existence of unreacted substances is avoided, and therefore the purity and the yield are improved.

The present invention provides a preparation method of tilpoitide, belongs to the technical field of polypeptide synthesis, the preparation method adopts a small amount of lysate for cracking, and uses a small amount of poor solution composed of methyl tert-butyl ether and n-heptane in a volume ratio of 1~2:1 to precipitate crude peptide, the precipitated particles are uniform and large, not easy to agglomerate, the crude peptide impurity level is lower, easy to subsequent purification steps, and the amount of waste liquid generated is small, the present invention also uses activator 7-(1H-pyrrolo[2,3-b]pyridin-1-yl)-1H-benzo[d][1,2,3]triazole-1-ol to activate amino acids, the coupling reaction degree is high, and the target peptide yield is high. A preparation method of tilpoitide provided by the present invention has the advantages of being simple, economical, capable of mass production, low impurity content, high purification yield, and high yield.

The invention relates to a preparation method of amino acid selectively protected Fmoc-His (Mmt) containing side chain amino groups, and belongs to the technical field of polypeptide synthesis. The preparation method comprises the following steps: protecting carboxyl of amino acid, a main chain and amino groups of side chains, removing under specific conditions to obtain a corresponding product with protected amino groups of the side chains, and protecting amino groups of the main chain to realize synthesis of the high-purity histidine derivative. According to the method, the total yield can reach 78%, the product purity is larger than 99.8%, the chiral integrity is larger than 99.95%, the COD value of process wastewater is reduced by 62% compared with that of a traditional method, and the method is suitable for industrial production of polypeptide drugs such as long-acting insulin analogues. The amino acid preparation method provided by the invention is also suitable for lysine / histidine / ornithine / 2.3-diaminopropionic acid / tryptophan and the like.

The invention belongs to the technical field of polypeptide preparation methods, and particularly relates to a method for chemically synthesizing glycosylated insulin. The preparation method comprises the following steps: preparing an insulin chain A by using a solid-phase polypeptide synthesis technology, selectively generating an intrachain disulfide bond A6-A11 in a post-treatment process of resin, preparing a glycosylated insulin chain B by using sugar amino acid, connecting the chain A and the chain B by forming an A20-B19 disulfide bond, then generating an A7-B7 disulfide bond, and preparing a glycosylated insulin chain B by using a solid-phase polypeptide synthesis technology. And the protecting group of the sugar is removed by using development conditions in the proper steps to obtain the glycosylated insulin. According to the method disclosed by the invention, the formation of disulfide bonds is accurately controlled, the product purity is higher, and the synthesis yield is higher. Moreover, the method also provides a sugar deprotection strategy with sialic acid methyl ester, so that the preparation of the glycosylated insulin is realized.

The invention relates to a method for preparing Fmoc-Lys (R)-OH fragment peptide by a solid phase method, and belongs to the technical field of peptide synthesis. According to the method, a solid-phase synthesis process route is adopted, 2-CTC lipid is taken as a solid-phase carrier, an initial material Dde-Lys-FMOC is adopted, any amino acid can be coupled to side chain amino groups in sequence, after coupling is completed, hydrazine hydrate is adopted for reduction removal of Dde and FMOC-0su cap exposure of amino groups, and finally, weak acid is adopted for cutting off full-protection peptide from resin, so that a target product crude peptide is obtained. The purity of the crude peptide prepared by the method reaches 95%, the purity can reach 99% or above through one-step extraction, the method avoids the problems of long liquid phase synthesis time and tedious procedures, and the product yield and the process stability are greatly improved.

The invention discloses a preparation method of a side chain Fmoc-His (Mtt), and relates to the technical field of polypeptide synthesis. The preparation method comprises the following steps: placing Fmoc-His-OH in a reaction bottle, adding a proper amount of solvent DCM, adding (CH3) 3SiCl, carrying out temperature-controlled reflux for 2 hours, then adding alkali Et3N / DIPEA as an acid-binding agent, and carrying out a reaction until the solution is clear; the temperature is controlled to be 10-20 DEG C, Mtt-Cl and Et3N / DIPEA are added in batches, the temperature is increased to 23-28 DEG C, the reaction is performed overnight, and Fmoc-His (Mtt) containing side chain amino is obtained; the final product of Fmoc-His (Mtt) is obtained through the steps of extraction, concentration, recrystallization, stirring and washing, filtration, drying and the like. When the molar ratio of the main raw materials Fmoc-His-OH to (CH3) 3SiCl to DIPEA to Mtt-Cl is 1: 1.5: 2.35: 1.15, the effect is optimal, the yield of the finally obtained Fmoc-His (Mtt) can reach 96% or above, and the purity is higher than 99%.

This invention discloses a rhodamine B-modified lysine derivative, its synthesis method, and its applications. The structural formula of the rhodamine B-modified lysine derivative is shown below. The invention first synthesizes Fmoc-Lys(Boc)-OtBu using commercially available Fmoc-Lys(Boc)-OH as a starting material. Then, after selectively removing the Boc protecting group from the side chain amino group, it condenses with rhodamine B to generate Fmoc-Lys(Rho)-OtBu. Finally, the tBu protecting group is removed to obtain Fmoc-Lys(Rho)-OH. The Fmoc-Lys(Rho)-OH synthesized by this invention can be loaded onto peptides using Fmoc solid-phase peptide synthesis technology for rapid and automated synthesis of rhodamine B-modified peptides.

The utility model relates to the technical field of polypeptide synthesis, and discloses a production-type continuous-flow polypeptide synthesis integrated column, including a positioning device, a supporting device is provided at the lower end of the positioning device, the positioning device includes a base, a plurality of bottom boxes are fixedly connected to the upper end of the base, the four corners of the upper end of the base are fixedly connected to fixed columns, the upper end of the fixed column is hinged with a support rod, the outer surfaces of both ends of the support rod are fixedly connected with a clamping block, and the upper end of the support rod is provided with a limit plate. The production-type continuous-flow polypeptide synthesis integrated column is achieved by erecting the support rod, using the clamping block to limit the limit plate, tightening the nut with the support rod thread to fix the limit plate, passing the integrated column through the limit plate and clamping it into the bottom box, then putting on a sleeve and rotating it, so that the sleeve and the limit plate thread rotate to position the integrated column, thereby achieving the effect of easy disassembly and assembly of the integrated column and convenient transportation.