CN104877016A - Folded chlorotoxin, chlorotoxin mutant, folded chlorotoxin mutant and preparation process thereof - Google Patents
Folded chlorotoxin, chlorotoxin mutant, folded chlorotoxin mutant and preparation process thereof Download PDFInfo
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- CN104877016A CN104877016A CN201510218160.8A CN201510218160A CN104877016A CN 104877016 A CN104877016 A CN 104877016A CN 201510218160 A CN201510218160 A CN 201510218160A CN 104877016 A CN104877016 A CN 104877016A
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- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
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Abstract
The invention discloses a folded chlorotoxin, a chlorotoxin mutant, a folded chlorotoxin mutant and a preparation process thereof. The peptide sequence of the folded chlorotoxin is MCMPCFTTDHQMARKCDDCCGGKGRGKCYGPQCLCR-NH2. The peptide sequence of folded chlorotoxin mutant is MCMPCFTTDHQMARSCDDCCGGSGRGSCYGPQCLCR-NH2, and the folded chlorotoxin mutant is formed by replacing lysine (Lys, K) inside the peptide sequence of the chlorotoxin with serine (Ser, S). According to the preparation process disclosed by the invention, the potential application value of the chlorotoxin and a ramification thereof in biology and pharmacy can be extended, and good economic benefit and social benefit on the aspects of lift health, individual medical treatment and the like can be achieved.
Description
Technical field
The present invention relates to a kind of folding chloro toxin, chloro toxin varient and folding chloro toxin varient and preparation technology thereof.
Background technology
One section of polypeptide be made up of 36 amino-acid residues is found in recent years by scholar---chloro toxin (chlorotoxin is called for short CTX).This CTX has good tumor-targeting, can specific binding kinds of tumor cells, as neurospongioma, malignant sarcomas, intestinal cancer and prostate cancer etc.Research shows, CTX enters tumour cell by MMP-2 (MMP-2) mediation, and MMP-2 only expresses in tumor cell surface a large amount, and normal cell surface is not expressed, and this explains the reason of CTX specific binding tumour cell.Meanwhile, although research display CTX has strong toxicity to invertebrates, nontoxic to Mammals.The existing radiotherapeutic agent 131I-TM-601 utilizing CTX to modify at present, is accepting FDA examination & approval, and is entering the II clinical trial phase stage.Also have research that CTX is connected the tumor imaging etc. being used for surgical procedure with fluorescence dye.Therefore, CTX may become the very high target head base of a kind of tumour-specific.
The research direction of current educational circles is all based on chloro toxin (chlorotoxin), and lacks research and innovation for the pleated sheet structure of its chloro toxin and variant structure, therefore, limits the application potential of chloro toxin.
Summary of the invention
First object of the present invention is the shortcoming and defect existed to overcome prior art, and provides a kind of folding chloro toxin.
Second object of the present invention is to provide a kind of preparation technology of above-mentioned folding chloro toxin.
3rd object of the present invention is to provide a kind of chloro toxin varient.
4th object of the present invention is to provide a kind of folding chloro toxin varient.
5th object of the present invention is to provide a kind of preparation technology of above-mentioned folding chloro toxin varient.
For realizing first object of the present invention, for realizing first object of the present invention, technical scheme of the present invention is its peptide sequence is MCMPCFTTDHQMARKCDDCCGGKGRGKCYGPQCLCR-NH2;
Its structural formula is:
For realizing second object of the present invention, technical scheme of the present invention includes following steps:
Reaction system is built: weighed by the chloro toxin of 40 milligrams and be placed in the container being placed with 100 mmole bicarbonate of ammonia, 2-4 mmole Guanidinium hydrochloride, 10-200 mmole gsh, 10wt% methyl-sulphoxide mixing solutions in such as the following ratio;
By reaction system vortex oscillation until the transparent clarification of solution, reaction system is placed in 4 degrees Celsius of refrigerating chambers, reaction 1-24 hour, obtains folding chloro toxin production.
For realizing second object of the present invention, technical scheme of the present invention can also comprise the following steps:
Build reaction system by following numerical value equal proportion: chloro toxin weigh be placed on be placed with 100 mmole bicarbonate of ammonia, 2 mmole disodium ethylene diamine tetraacetate, 3 mmole reduced glutathiones, 1 mmole oxidized glutathione, acidity-basicity ph ~ 7.8 mixing solutions container in, in reaction system, chloro toxin concentration is 0.05 mg/ml;
By reaction system vortex oscillation until the transparent clarification of solution, reaction system is placed in 4 degrees Celsius of refrigerating chambers, reacts 6 days, obtains folding chloro toxin production.
For realizing the 3rd goal of the invention of the present invention, to be the peptide sequence of this chloro toxin varient be technical scheme of the present invention:
MCMPCFTTDHQMARSCDDCCGGSGRGSCYGPQCLCR-NH2；
Its Methionin (Lys, K) replaced in chloro toxin peptide sequence by Serine (Ser, S) is formed, and its structural formula is:
For realizing the 4th object of the present invention, technical scheme of the present invention is
The peptide sequence of this folding chloro toxin varient is:
MCMPCFTTDHQMARSCDDCCGGSGRGSCYGPQCLCR-NH2；
It replaces Methionin (Lys, K) in chloro toxin peptide sequence by Serine (Ser, S) and forms,
The structural formula of this folding chloro toxin varient is:
For realizing the 5th object of the present invention, technical scheme of the present invention comprises the following steps:
Reaction system is built: 38 milligrams of chloro toxin varients weigh and are placed in the container being placed with 100 mmole bicarbonate of ammonia, 2-4 mmole Guanidinium hydrochloride, 10-200 mmole gsh, 10wt% methyl-sulphoxide mixing solutions by following numerical value equal proportion;
By reaction system vortex oscillation until the transparent clarification of solution, reaction system is placed in 4 degrees Celsius of refrigerating chambers, reaction 1-24 hour, obtains folding chloro toxin varient product.
For realizing the 5th object of the present invention, technical scheme of the present invention can also be comprise the following steps:
Build reaction system by following numerical value equal proportion: chloro toxin varient weigh be placed on be placed with 100 mmole bicarbonate of ammonia, 2 mmole disodium ethylene diamine tetraacetate, 3 mmole reduced glutathiones, 1 mmole oxidized glutathione, acidity-basicity ph ~ 7.8 mixing solutions container in, in reaction system, chloro toxin varient concentration is 0.05 mg/ml
By reaction system vortex oscillation until the transparent clarification of solution, reaction system is placed in 4 degrees Celsius of refrigerating chambers, reacts 6 days, obtains folding chloro toxin varient product.
Chloro toxin varient of the present invention and folding chloro toxin varient have potential using value in biology with pharmacy, chloro toxin varient and folding chloro toxin varient are expected to be more widely used for fields such as the body internal labeling of target tumor Clinics and Practices, molecular probe and spike, drug metabolism, screening and optimizations in cancer cell selectivity binding, the further targeting sustained and controlled release of raising medicine and the accuracy of cancer operation, produce good economic and social profit for the aspect such as life and health and personalized medicine.
In addition, synthetic technological condition of the present invention is gentle, Separation & Purification simple process, easily realizes Automated condtrol, technique environmental protection.
Below in conjunction with specification drawings and specific embodiments, the present invention is described further.
Accompanying drawing explanation
Under Fig. 1 embodiment of the present invention 1 different condition, chloro toxin folds the high performance liquid phase separation spectrogram of reaction;
Under Fig. 2 embodiment of the present invention 2 different condition, chloro toxin folds the high performance liquid phase separation spectrogram of reaction;
Under Fig. 3 embodiment of the present invention 3 different condition, chloro toxin folds the high performance liquid phase separation spectrogram of reaction;
Under Fig. 4 embodiment of the present invention 4 different condition, chloro toxin folds the high performance liquid phase separation spectrogram of reaction;
Under Fig. 5 embodiment of the present invention 5 different condition, chloro toxin folds high performance liquid phase separation and the mass spectrum of reaction;
In Fig. 6 embodiment of the present invention 6, chloro toxin varient solid phase synthesis high performance liquid phase is separated and identifies with LC-MS;
Under Fig. 7 embodiment of the present invention 7 different condition, chloro toxin varient folds the high performance liquid phase separation spectrogram of reaction;
Under Fig. 8 embodiment of the present invention 8 different condition, chloro toxin varient folds high performance liquid phase separation and the mass spectrum of reaction.
Embodiment
1-8 by reference to the accompanying drawings; below by embodiment, the present invention is specifically described; only be used to further illustrate the present invention; can not be interpreted as limiting the scope of the present invention, the technician in this field can make some nonessential improvement and adjustment according to the content of foregoing invention to the present invention.
Embodiment 1: chloro toxin (40 milligrams) weighs and is placed in the test tube being placed with 100 mmole bicarbonate of ammonia, 2 mmole Guanidinium hydrochlorides, 10 mmole gsh, 10% methyl-sulphoxide mixing solutions, and vortex oscillation at least 3 times is until the transparent clarification of solution.System is placed in 4 degrees Celsius of refrigerating chambers, takes out product in different time points (1 hour, 2 hours, 4 hours, 6 hours, 10 hours, 24 hours).High performance liquid chromatography with Dionex C18 Acclaim 120 analytical column for chromatography column, flow velocity 1.00 ml/min, wash-out is mutually: 0.1% trifluoroacetic acid aqueous solution; 0.1% trifluoroacetic acid acetonitrile solution, 5-65% gradient elution 30 minutes, obtains the separation spectrogram of folding chloro toxin.
Embodiment 2: chloro toxin (40 milligrams) weighs and is placed in the test tube being placed with 100 mmole bicarbonate of ammonia, 4 mmole Guanidinium hydrochlorides, 10 mmole gsh, 10% methyl-sulphoxide mixing solutions, and vortex oscillation at least 3 times is until the transparent clarification of solution.System is placed in 4 degrees Celsius of refrigerating chambers, takes out product in different time points (3 hours, 7 hours, 24 hours).High performance liquid chromatography with Dionex C18 Acclaim 120 analytical column for chromatography column, flow velocity 1.00 ml/min, wash-out is mutually: 0.1% trifluoroacetic acid aqueous solution; 0.1% trifluoroacetic acid acetonitrile solution, 5-65% gradient elution 30 minutes, obtains the separation spectrogram of folding chloro toxin.
Embodiment 3: chloro toxin (40 milligrams) weighs and is placed in the test tube being placed with 100 mmole bicarbonate of ammonia, 2 mmole Guanidinium hydrochlorides, 100 mmole gsh, 10% methyl-sulphoxide mixing solutions, and vortex oscillation at least 3 times is until the transparent clarification of solution.System is placed in 4 degrees Celsius of refrigerating chambers, takes out product in different time points (3 hours, 7 hours, 24 hours).High performance liquid chromatography with Dionex C18 Acclaim 120 analytical column for chromatography column, flow velocity 1.00 ml/min, wash-out is mutually: 0.1% trifluoroacetic acid aqueous solution; 0.1% trifluoroacetic acid acetonitrile solution, 5-65% gradient elution 30 minutes, obtains the separation spectrogram of folding chloro toxin.
Embodiment 4: chloro toxin (40 milligrams) weighs and is placed in the test tube being placed with 100 mmole bicarbonate of ammonia, 2 mmole Guanidinium hydrochlorides, 200 mmole gsh, 10% methyl-sulphoxide mixing solutions, and vortex oscillation at least 3 times is until the transparent clarification of solution.System is placed in 4 degrees Celsius of refrigerating chambers, takes out product in different time points (3 hours, 7 hours).High performance liquid chromatography with Dionex C18 Acclaim 120 analytical column for chromatography column, flow velocity 1.00 ml/min, wash-out is mutually: 0.1% trifluoroacetic acid aqueous solution; 0.1% trifluoroacetic acid acetonitrile solution, 5-65% gradient elution 30 minutes, obtains the separation spectrogram of folding chloro toxin.
Embodiment 5: chloro toxin weigh be placed on be placed with 100 mmole bicarbonate of ammonia, 2 mmole disodium ethylene diamine tetraacetate, 3 mmole reduced glutathiones, 1 mmole oxidized glutathione, acidity-basicity ph=7.8 mixing solutions test tube in (chloro toxin concentration is 0.05 mg/ml), vortex oscillation at least 3 times is until the transparent clarification of solution.System is placed in 4 degrees Celsius of refrigerating chambers, takes out product after 6 days.High performance liquid chromatography with Dionex C18 Acclaim 120 analytical column for chromatography column, flow velocity 1.00 ml/min, wash-out is mutually: 0.1% trifluoroacetic acid aqueous solution; 0.1% trifluoroacetic acid acetonitrile solution, 5-65% gradient elution 30 minutes, be separated the folding chloro toxin obtaining purifying, retention time is 22.8 minutes, yield 8%.Four groups of disulfide linkage of folding chloro toxin and formation split a point peak identification by Moldi-TOF mass spectrum.
Embodiment 6: amino acid is weighed by sequence (MCMPCFTTDHQMARSCDDCCGGSGRGSCYGPQCLCR-NH2) equal proportion and is placed in solid phase synthetic instrument filling tube, weigh 3-10 times of resin in reactor, open Solid-phase synthesis peptides, reaction stopped after 24-36 hour.Crude product shifted suction filtration, wash-out, go protection, and with freezing washed with diethylether, centrifugal, vacuum-freeze-dry.With crude product at high performance liquid chromatography sample introduction, be separated with Vydac C18 semipreparative column, flow velocity 3.00 ml/min, wash-out is mutually: 0.1% trifluoroacetic acid aqueous solution; 0.1% trifluoroacetic acid acetonitrile solution, 5-65% gradient elution 30 minutes, be separated the chloro toxin varient obtaining purifying, retention time is 19.8 minutes, yield 12%.Chloro toxin varient by LC-ESI liquid chromatograph mass spectrography device by splitting a point peak identification.
Embodiment 7: chloro toxin varient (38 milligrams) weighs and is placed in the test tube being placed with 100 mmole bicarbonate of ammonia, 2 mmole Guanidinium hydrochlorides, 200 mmole gsh, 10% methyl-sulphoxide mixing solutions, and vortex oscillation at least 3 times is until the transparent clarification of solution.System is placed in 4 degrees Celsius of refrigerating chambers, takes out product after 24 hours.High performance liquid chromatography with Dionex C18 Acclaim 120 analytical column for chromatography column, flow velocity 1.00 ml/min, wash-out is mutually: 0.1% trifluoroacetic acid aqueous solution; 0.1% trifluoroacetic acid acetonitrile solution, 5-65% gradient elution 30 minutes, obtains the separation spectrogram of folding chloro toxin.
Embodiment: 8: chloro toxin varient weigh be placed on be placed with 100 mmole bicarbonate of ammonia, 2 mmole disodium ethylene diamine tetraacetate, 3 mmole reduced glutathiones, 1 mmole oxidized glutathione, acidity-basicity ph=7.8 mixing solutions test tube in (chloro toxin varient concentration is 0.05 mg/ml), vortex oscillation at least 3 times is until the transparent clarification of solution.System is placed in 4 degrees Celsius of refrigerating chambers, takes out product after 6 days.High performance liquid chromatography with Dionex C18 Acclaim 120 analytical column for chromatography column, flow velocity 1.00 ml/min, wash-out is mutually: 0.1% trifluoroacetic acid aqueous solution; 0.1% trifluoroacetic acid acetonitrile solution, 5-65% gradient elution 30 minutes, be separated the folding chloro toxin varient obtaining purifying, retention time is 23.5 minutes, yield 7%.Four groups of disulfide linkage of folding chloro toxin varient and formation split a point peak identification by Moldi-TOF mass spectrum.
Claims (7)
1. a folding chloro toxin, is characterized in that: its peptide sequence is MCMPCFTTDHQMARKCDDCCGGKGRGKCYGPQCLCR-NH2;
Its structural formula is:
。
2. a preparation technology for folding chloro toxin as claimed in claim 1, is characterized in that including following steps:
Reaction system is built: weighed by the chloro toxin of 40 milligrams and be placed in the container being placed with 100 mmole bicarbonate of ammonia, 2-4 mmole Guanidinium hydrochloride, 10-200 mmole gsh, 10wt% methyl-sulphoxide mixing solutions by following numerical value equal proportion;
By reaction system vortex oscillation until the transparent clarification of solution, reaction system is placed in 4 degrees Celsius of refrigerating chambers, reaction 1-24 hour, obtains folding chloro toxin production.
3. a preparation technology for folding chloro toxin as claimed in claim 1, is characterized in that including following steps:
Build reaction system by following numerical value equal proportion: chloro toxin weigh be placed on be placed with 100 mmole bicarbonate of ammonia, 2 mmole disodium ethylene diamine tetraacetate, 3 mmole reduced glutathiones, 1 mmole oxidized glutathione, acidity-basicity ph ~ 7.8 mixing solutions container in, in reaction system, chloro toxin concentration is 0.05 mg/ml;
By reaction system vortex oscillation until the transparent clarification of solution, reaction system is placed in 4 degrees Celsius of refrigerating chambers, reacts 6 days, obtains folding chloro toxin production.
4. a chloro toxin varient, is characterized in that:
The peptide sequence of this chloro toxin varient is:
MCMPCFTTDHQMARSCDDCCGGSGRGSCYGPQCLCR-NH2；
Its Methionin (Lys, K) replaced in chloro toxin peptide sequence by Serine (Ser, S) is formed, and its structural formula is:
。
5. a folding chloro toxin varient, is characterized in that:
The peptide sequence of this folding chloro toxin varient is:
MCMPCFTTDHQMARSCDDCCGGSGRGSCYGPQCLCR-NH2；
It replaces Methionin (Lys, K) in chloro toxin peptide sequence by Serine (Ser, S) and forms,
The structural formula of this folding chloro toxin varient is:
。
6. a preparation technology for folding chloro toxin varient as claimed in claim 5, is characterized in that comprising the following steps:
Reaction system is built: 38 milligrams of chloro toxin varients weigh and are placed in the container being placed with 100 mmole bicarbonate of ammonia, 2-4 mmole Guanidinium hydrochloride, 10-200 mmole gsh, 10wt% methyl-sulphoxide mixing solutions by following numerical value equal proportion;
By reaction system vortex oscillation until the transparent clarification of solution, reaction system is placed in 4 degrees Celsius of refrigerating chambers, reaction 1-24 hour, obtains folding chloro toxin varient product.
7. a preparation technology for folding chloro toxin varient as claimed in claim 5, is characterized in that comprising the following steps:
Build reaction system by following numerical value equal proportion: chloro toxin varient weigh be placed on be placed with 100 mmole bicarbonate of ammonia, 2 mmole disodium ethylene diamine tetraacetate, 3 mmole reduced glutathiones, 1 mmole oxidized glutathione, acidity-basicity ph ~ 7.8 mixing solutions container in, in reaction system, chloro toxin varient concentration is 0.05 mg/ml
By reaction system vortex oscillation until the transparent clarification of solution, reaction system is placed in 4 degrees Celsius of refrigerating chambers, reacts 6 days, obtains folding chloro toxin varient product.
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Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN106995493A (en) * | 2010-02-04 | 2017-08-01 | 摩尔弗泰克有限公司 | Catilan polypeptide and conjugate and its application |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20120183544A1 (en) * | 1995-12-27 | 2012-07-19 | The Uab Research Foundation | Diagnosis and treatment of neuroectodermal tumors |
| CN102844044A (en) * | 2010-02-04 | 2012-12-26 | 摩尔弗泰克有限公司 | Chlorotoxin polypeptides and conjugates and uses thereof |
-
2015
- 2015-04-30 CN CN201510218160.8A patent/CN104877016A/en active Pending
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20120183544A1 (en) * | 1995-12-27 | 2012-07-19 | The Uab Research Foundation | Diagnosis and treatment of neuroectodermal tumors |
| CN102844044A (en) * | 2010-02-04 | 2012-12-26 | 摩尔弗泰克有限公司 | Chlorotoxin polypeptides and conjugates and uses thereof |
Non-Patent Citations (2)
| Title |
|---|
| G. LIPPENS ET AL.: "NMR Sequential Assignments and Solution Structure of Chlorotoxin, a Small Scorpion Toxin That Blocks Chloride Channels", 《BIOCHEMISTRY》 * |
| 周艳荣等: "肽合成中多对二硫键的形成策略及分析方法", 《生物技术通讯》 * |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN106995493A (en) * | 2010-02-04 | 2017-08-01 | 摩尔弗泰克有限公司 | Catilan polypeptide and conjugate and its application |
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Application publication date: 20150902 |