# US 9,518,099 B1 · Refolded chlorotoxin, chlorotoxin variant, refolded chlorotoxin variant, and preparation technology thereof

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- Number: US 9,518,099 B1
- Document ID: US9518099B1
- Status: Granted
- Kind: B1
- Application number: 14/852,619
- Filed: 2015-09-13
- Granted: 2016-12-13
- Earliest claimed: 2015-09-13
- Assignees: Wenzhou Institute of Biomaterials and Engineering
- Applicants: Wenzhou Institute of Biomaterials and Engineering
- Inventors: Zhe Liu
- Web page: https://patentgrep.com/patent/US9518099B1

## CPC

- C07K 14/43522: {from scorpions}
- C07K: PEPTIDES (peptides in foodstuffs A23; obtaining protein compositions for foodstuffs, working-up proteins for foodstuffs A23J; preparations for medicinal purposes A61K; peptides containing beta-lactam rings C07D; cyclic dipeptides not having in their molecule any other peptide link than those which form their ring, e.g. piperazine-2,5-diones, C07D; ergot alkaloids of the cyclic peptide type C07D519/02; macromolecular compounds having statistically distributed amino acid units in their molecules, i.e. when the preparation does not provide for a specific; but for a random sequence of the amino acid units, homopolyamides and block copolyamides derived from amino acids C08G69/00; macromolecular products derived from proteins C08H1/00; preparation of glue or gelatine C09H; single cell proteins, enzymes C12N; genetic engineering processes for obtaining peptides C12N15/00; compositions for measuring or testing processes involving enzymes C12Q; investigation or analysis of biological material G01N33/00)

## Abstract

Disclosed are a folded chlorotoxin, a chlorotoxin variant and a folded chlorotoxin variant and their preparation technology. The folded chlorotoxin has a peptide sequence of MCMPCFTTDHQMARKCDDCCGGKGRGKCYGPQCLCR-NH2, and the folded chlorotoxin variant has a peptide sequence of MCMPCFTTDHQMARSCDDCCGGSGRGSCYGPQCLCR-NH2 and is formed by replacing serine (Ser, S) by lysine (Lys, K) in the peptide sequence of chlorotoxin. The chlorotoxin and its derivatives have potential application values in biological and medical fields and good economic and social benefits to life, health, and personalized healthcare.

## Claims

### Claim 1

A preparation technology of a folded chlorotoxin with a peptide sequence of MCMPCFTTDHQMARKCDDCCGGKGRGKCYGPQCLCR-NH2 and a structural formula of:
comprising the steps of:
creating a reacting system according to the following proportion of numeric values by weighing 40 mg of chlorotoxin, and putting the chlorotoxin in a container containing a mixed solution of 100 Mmol bicarbonate, 2˜4 Mmol guanidine hydrochloride, 10˜200 Mmol glutathione, and 10 wt % dimethylsulfoxide; and
vortexing the reacting system until the solution becomes transparent and clear, and setting the reacting system in a refrigerating chamber at 4 degrees C. for a reaction of 1˜24 hours to obtain a folded chlorotoxin product.

### Claim 2

A preparation technology of a folded chlorotoxin with a peptide sequence of MCMPCFTTDHQMARKCDDCCGGKGRGKCYGPQCLCR-NH2 and a structural formula of:
comprising the steps of:
creating a reacting system according to the following proportion of numeric values by weighing the chlorotoxin and putting the chlorotoxin in a container containing a mixed solution of 100 Mmol bicarbonate, 2 Mmol disodium edetate, 3 Mmol reduced glutathione, 1 Mmol oxidized glutathione and having a pH˜7.8, wherein the reacting system has a chlorotoxin concentration of 0.05 mg/ml; and
vortexing the reacting system until the solution becomes transparent and clear, and setting the reacting system in a refrigerating chamber at 4 degrees C. for a reaction of 6 days to obtain a folded chlorotoxin product.