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23 results about "Conotoxin" patented technology

A conotoxin is one of a group of neurotoxic peptides isolated from the venom of the marine cone snail, genus Conus. Conotoxins, which are peptides consisting of 10 to 30 amino acid residues, typically have one or more disulfide bonds. Conotoxins have a variety of mechanisms of actions, most of which have not been determined. However, it appears that many of these peptides modulate the activity of ion channels. Over the last few decades conotoxins have been the subject of pharmacological interest.

Anti-aging composition for reducing stress-type fatigue and preparation method and application thereof

The application relates to the cosmetic technical field, and particularly discloses an anti-aging composition for reducing stress fatigue, a preparation method and application thereof. The anti-aging composition comprises a camellia chrysantha extract, a prosopis juliflora seed extract, a mu-conotoxin and an ascorbic acid polypeptide; the mass ratio of the camellia chrysantha extract, the prosopis juliflora seed extract, the mu-conotoxin and the ascorbic acid polypeptide is (0.1-5):(0.01-2):(0.001-1):(0.01-5). The anti-aging composition provided by the application can reduce stress damage of skin cells, improve cell vitality, thereby improving the problems of skin dullness, roughness, looseness and fine lines caused by overwork, work and emotional stress, and is mild and non-irritating, and is suitable for sensitive skin people.
Owner:N O D TOPIA (GUANGZHOU) BIOTECHNOLOGY CO LTD

Mu-conotoxin KIIIA mutant rich in positive charges and application thereof

The invention belongs to the technical field of biological medicines, and relates to a mutants of mu-conotoxin KIIIA rich in positive charges and application of the mutants. The mutant is obtained by implementing site-specific mutagenesis at the following positions on a mutant as shown in SEQ ID NO.1 in a sequence table: S6R; the amino acid sequence of the mutant is as shown in SEQ ID NO. 2 in a sequence table. According to the invention, systematic structural optimization is carried out on a parent peptide KIIIA containing three pairs of disulfide bonds, and a strategy of combining disulfide bond deletion and amino acid site-directed mutagenesis is adopted, so that a mutant which is simple and convenient to synthesize and has a remarkable inhibition effect on a NaV1.4 channel is obtained. The mutant has high activity, high stability and better pharmacokinetic characteristics, and has wide development potential.
Owner:OCEAN UNIV OF CHINA

μ-conotoxin peptide cniiic mutant and use thereof

PCT designated stageWO2025256232A1Cosmetic preparationsNervous disorderMuscle tissueConotoxin
Provided are a μ-conotoxin peptide CnIIIC mutant and the use thereof. Further provided are a nucleic acid construct of the μ-conotoxin peptide CnIIIC mutant, and an expression vector and transformed cell thereof, and the use thereof. The μ-conotoxin peptide CnIIIC mutant has an enhanced transdermal penetration ability, and can effectively penetrate the skin barrier to directly act on nerves and muscle tissues in the underlying layer of skin. By means of the unique physical and chemical properties, the mutant can realize a local pharmaceutical effect within a relatively short period of time, thereby greatly improving the bioavailability of a drug.
Owner:PEPTIORIGIN BIOTECHNOLOGY CO LTD

A skin care composition for improving menopausal aging in women and use thereof

The present application relates to a kind of skin care composition for improving female menopausal aging and its application, the skin care composition for improving female menopausal aging includes the following components: conotoxin peptide, bakuchiol, alfalfa extract and radix pseudostellariae extract, the weight ratio of conotoxin peptide, bakuchiol, alfalfa extract and radix pseudostellariae extract is (0.1-5) :(0.1-3) :(0.1-5) :(0.1-3). The four are by means of inhibiting neurotransmitter, regulating hormone etc., enhance skin health, effectively improve the problem of menopausal female skin aging, make skin firm and smooth.
Owner:N O D TOPIA (GUANGZHOU) BIOTECHNOLOGY CO LTD

Mu-conotoxin KIIIA mutant rich in positive charges and application thereof

The invention belongs to the technical field of biological medicines, and relates to a mutants of mu-conotoxin KIIIA rich in positive charges and application of the mutants. The mutant is obtained by carrying out site-directed mutagenesis on C1A, K7R and C15R on a natural mu-conotoxin KIIIA sequence; the amino acid sequence of the mutant is shown as SEQ ID NO. 1 in a sequence table. According to the invention, a series of mutants which are simple and convenient to synthesize and have a remarkable inhibition effect on a NaV1.4 channel are obtained by performing systematic structural optimization on a parent peptide KIIIA containing three pairs of disulfide bonds and adopting a strategy of combining disulfide bond deletion and amino acid site-directed mutagenesis. Furthermore, non-natural amino acid Pen is introduced into the mutant with the optimal activity, so that the stability of the mutant in vivo is remarkably enhanced, and the action time is prolonged.
Owner:OCEAN UNIV OF CHINA

Method for separating and purifying recombinant conopeptide through one-step chromatography and application thereof

The invention provides a method for rapidly preparing recombinant conopeptide through one-step chromatography and application. According to the method disclosed by the invention, after fermentation liquor of conopeptide subjected to recombinant expression of a pichia pastoris system is subjected to crude purification, the refined purification of the conopeptide subjected to enzyme digestion is completed only through a one-step cation chromatography method, and the high-purity conopeptide with the purity of 98% or above is obtained. The invention further finds that the conopeptide biosynthesized by using a pichia pastoris expression system has the characteristics of high yield and easiness in large-scale production, the TrxA tag protein is screened and adopted, so that folding and expression of the recombinant conopeptide are efficiently promoted, and the TrxA tag protein has oxidation-reduction activity, so that a suitable environment is provided for formation of disulfide bonds of the conopeptide, and the conopeptide has a good application prospect. The problem of disulfide bond mismatching is obviously reduced. The invention provides an effective solution for biosynthesis and large-scale production of conopeptide.
Owner:JIANGSU YAOHAI NUOXIN BIOTECHNOLOGY CO LTD

Superoxide dismutase / mu-conotoxin sustained-release compound based on galactomannan covalent shell layer and application of superoxide dismutase / mu-conotoxin sustained-release compound

The invention belongs to the technical field of biological medicines, and relates to a superoxide dismutase / mu-conotoxin sustained-release compound based on a galactomannan covalent shell and application of the superoxide dismutase / mu-conotoxin sustained-release compound. Galactomannan in the compound is oxidized by NaIO4 and is coupled with stearic acid to form a stearic acid-oxidized galactomannan shell-core structure, mu-conotoxin is connected with galactomannan through a covalent bond, superoxide dismutase is loaded into the shell-core structure, and the structural formula of the compound is as follows: SA-O-CM-mu-CnIIICn / SODm. Wherein n is a natural number from 3 to 11, and m is a natural number from 1 to 8. The SOD and the mu-CnIII C are loaded into the galactomannan covalent shell layer, so that the stability and the biological activity of the SOD and the mu-CnIII C can be effectively improved, degradation of hydrolase on protein and polypeptide is resisted, and the compound is endowed with excellent antioxidant, anti-wrinkle, anti-inflammatory and anti-radiation activity.
Owner:SHANDONG UNIV +1

Mu-type conotoxin peptide, polynucleotide coded by mu-type conotoxin peptide and application of mu-type conotoxin peptide

The invention discloses a mu-type conotoxin peptide, polynucleotide encoded by the mu-type conotoxin peptide and application of the mu-type conotoxin peptide. The amino acid sequence of the mu-type conotoxin peptide is shown as SEQ ID NO. 1. The invention provides a mu-type conotoxin peptide with higher biological activity than wild-type mu-type conotoxin, which can specifically block a Nav1.4 channel and reduce muscle contraction so as to be helpful for preventing and reducing wrinkles, and also can provide local anesthesia and reduce muscle activity, thereby playing an important role in the fields of beauty and medical treatment.
Owner:PEPTIORIGIN BIOTECHNOLOGY CO LTD

An eye essence cream and a preparation method thereof

The application relates to the technical field of eye care products, and particularly discloses an eye essence cream and a preparation method thereof. The eye essence cream comprises a moisturizing agent, an antioxidant, a penetration promoter, a viscosity regulator, an emulsifier, an emollient, a thickening agent, Coffea arabica seed oil, Baphia nitida bark extract, an anti-wrinkle composition, a Mei flower extract, a Pediococcus / Parsnip root ferment filtrate, an Adzuki bean seed extract, caprylyl glycol, acetyl hexapeptide-8, acetyl tetrapeptide-2, lactose, whey protein, lactic acid and the like. The anti-wrinkle composition is prepared by mixing acetyl hexapeptide-8, conotoxin, Hedychium spicatum extract, palmitoyl tripeptide-1 and palmitoyl tetrapeptide-7. The eye essence cream provided by the application has a comprehensive and efficient improvement effect on complex problems such as dry skin, fine lines, relaxation, dark circles and eye bags.
Owner:ZHEJIANG YINGSHU BIOTECHNOLOGY CO LTD

Preparation method and application of terpene alcohol of permeation-promoting conopeptide

The invention discloses a preparation method and application of a terpene alcohol body of permeation-enhancing conopeptide, and belongs to the technical field of cosmetics. The terpene alcohol body for enhancing the permeation of conopeptide provided by the invention comprises the following components in percentage by mass: 1 to 15 percent of phospholipid, 0.1 to 10 percent of lysophosphatidylcholine, 0.5 to 3 percent of cholesterol, 0.01 to 2 percent of terpene, 2 to 50 percent of polyhydric alcohol, 0.001 to 1 percent of conopeptide and the balance of deionized water. On the basis of molecular docking, phospholipid and lysophosphatidylcholine with specific types and proportions are screened and used for entrapment of conopeptide, and terpene alcohol with stable structure and conopeptide entrapment efficiency greater than 90% is obtained; according to the preparation method, a terpenol body is added, a lysophosphatidylcholine, terpene and polyhydric alcohol ternary permeation enhancing system is uniformly integrated to the terpenol body, finally, the transdermal capacity of conopeptide is remarkably enhanced, the transdermal depth of conopeptide is promoted, the intradermal cumulant of conopeptide is increased, and a foundation is laid for achieving the effect of the conopeptide in cosmetics.
Owner:JIANGNAN UNIV

Conotoxin polypeptide with single disulfide bond and mutant and application of conotoxin polypeptide

The invention belongs to the technical field of biological medicines, and relates to a spiro polypeptide with a single disulfide bond and a mutant and application thereof. The amino acid sequence of the conotoxin polypeptide is shown as SEQ ID NO.1 in a sequence table. One or more amino acid site-directed mutagenesis is carried out on the amino acid sequence of the conotoxin polypeptide to obtain a series of mutants. A plurality of mutants have better inhibitory activity and selectivity on an alpha9alpha10 acetylcholine receptor; wherein the IC50 of the M16R is 28.2 nM, and the IC50 of the F19R is 17.5 nM. In addition, M16R and F19R show in-vivo analgesic activity in a chemotherapeutic drug oxaliplatin induced rat crymodynia model, and have the potential of being developed into a neuropathic pain treatment drug targeting alpha9alpha10nAChR.
Owner:OCEAN UNIV OF CHINA

Preparation method of mu-conotoxin disulfide bond substitute

The invention provides a preparation method of a [mu]-conotoxin disulfide bond substitute, which comprises the following steps: on the basis of Fmoc solid-phase synthesis and DADA module embedding technology, coupling amino acid residues under the assistance of automatic microwaves to prepare a linear precursor peptide of [mu]-conotoxin, and carrying out in-situ oxidation and thiolysis activation on the linear precursor peptide to obtain the [mu]-conotoxin disulfide bond substitute. And carrying out folding oxidation on the obtained cyclized peptide by using natural chemical connection to assist cyclization so as to form the mu-conotoxin disulfide bond substitute. According to the method, the three-dimensional conformation and biological activity of the natural peptide are kept, meanwhile, efficient and rapid synthesis of the large-span disulfide bond substituted bridging peptide is achieved, the structural stability of the peptide product is remarkably improved, the reaction condition is mild and easy to control, the process is simple, the separation yield of the target product is stable, and the method can be used for rapidly preparing various variants and has wide application prospects. Different production and research requirements are met, and good market application prospects are achieved.
Owner:TSINGHUA UNIVERSITY +1

Mu-conopeptide fusion protein and preparation method of Mu-conopeptide

The invention provides a mu-conopeptide fusion protein and a preparation method of mu-conopeptide, and belongs to the technical field of biology. The invention provides a [mu]-conopeptide fusion protein. The [mu]-conopeptide fusion protein comprises a folded protein in a connected state and [mu]-conopeptide which is repeatedly connected in series, the folded protein comprises thioredoxin and disulfide bond isomerase; the amino acid sequence of the mu-conopeptide is as shown in SEQ ID NO: 1. According to the method disclosed by the invention, the thioredoxin and the disulfide bond isomerase are used as folding proteins, so that the tandem expressed mu-conopeptide can correctly and effectively form the mu-conopeptide with three pairs of disulfide bonds, and the method can effectively improve the yield of the mu-conopeptide. In addition, the [mu]-conopeptide fusion protein can be used for biosynthesizing [mu]-conopeptide, and compared with a traditional method, the [mu]-conopeptide fusion protein is more environmentally friendly, lower in cost compared with solid-phase synthesis and suitable for large-scale production.
Owner:SHENZHEN JINHE BIOLOGICAL CO LTD

Mutants of the positively charged mu-conotoxin kiiia and uses thereof

The application belongs to the technical field of biological medicine, and relates to a mutant of mu-conotoxin KIIIA rich in positive charges and application thereof. The mutant is obtained by performing C1A, K7R and C15R site-directed mutation on a natural mu-conotoxin KIIIA sequence; and the amino acid sequence of the mutant is shown in the sequence table SEQ ID NO. 1. The application performs systematic structural optimization on a parent peptide KIIIA containing three pairs of disulfide bonds, adopts a strategy of combining disulfide bond deletion with site-directed amino acid mutation, and obtains a synthetic simple mu-conotoxin KIIIA mutant which has a significant inhibitory effect on Na V 1.4 A series of mutants with significant inhibitory effect on the channel. Further by introducing non-natural amino acid Pen in the most active mutant, the stability in vivo is significantly enhanced, thereby prolonging the action time.
Owner:OCEAN UNIV OF CHINA

Mu-type conotoxin peptide mutant as well as pharmaceutical composition and application thereof

The invention discloses a mu-type conotoxin peptide mutant as well as a pharmaceutical composition and application thereof. The amino acid sequence of the mu-type conotoxin peptide mutant is as shown in SEQ ID NO. 1. Compared with a wild type mu-type conotoxin peptide, the mu-type conotoxin peptide [d-Arg2, Ser17]-dR-mu-CnIIIC disclosed by the invention has higher activity, the animal activity is improved by more than 20 times, and muscle contraction can be effectively reduced by specifically blocking a Nav1.4 channel. In addition, the compound can be used as a non-invasive anti-wrinkle treatment means to reduce or eliminate the formation of wrinkles on the human skin surface, and has a wide application prospect in the fields of medical treatment and beauty.
Owner:PEPTIORIGIN BIOTECHNOLOGY CO LTD

Construction method and application of engineering bacteria for producing conopeptide

The invention belongs to the field of genetic engineering and microbial pharmacy, and particularly relates to a construction method and application of engineering bacteria for producing conopeptide, and the construction method comprises the following steps: designing a gene segment for coding ketosteroid isomerase-Strep tag-conopeptide fusion protein, and the nucleotide sequence of the gene segment is as shown in SEQ ID NO: 2; the amino acid sequence of the ketosteroid isomerase-Strep tag-conopeptide fusion protein is as shown in SEQ ID NO: 1. Inserting the gene segment into multiple cloning sites of an expression vector to obtain a recombinant expression vector; and introducing the recombinant expression vector into escherichia coli competent cells through a chemical conversion method to obtain the engineering bacteria for producing conopeptide. According to the method, soluble efficient expression of conopeptide can be achieved, high-purity conopeptide is obtained through one-step affinity chromatography purification of the Strep tag, and the problems that in the prior art, conopeptide expression is difficult, and the purification process is complex are solved.
Owner:ZHEJIANG SEEDLING BIOTECHNOLOGY CO LTD

Mu-type conotoxin peptide [Ser17, Tyr11]-dR-Mu-CnIIIC and application thereof

The invention discloses a [mu] type conotoxin peptide [Ser17, Tyr11]-dR-[mu]-CnIIIC and an application thereof. The amino acid sequence of the mu-type conotoxin peptide is as shown in SEQ ID NO. 1. Compared with wild type mu-CnIIIC and [Ser17, Tyr11]-dR-mu-CnIIIC, the animal activity of the mu type conotoxin peptide disclosed by the invention is improved by 20 times, and meanwhile, the amino acid sequence composition of the [Ser17, Tyr11]-dR-mu-CnIIIC is reduced by 1 site compared with the wild type mu-CnIIIC, so that the synthesis cost can be further reduced.
Owner:PEPTIORIGIN BIOTECHNOLOGY CO LTD

An instant firming and anti-wrinkle composition and a method for preparing the same

The application discloses an instant firming and anti-wrinkle eye composition and a preparation method thereof. The composition comprises the following components: a moisturizing agent, a conotoxin, an acetylated chitosan, a hydroxypropyl tetrahydropyran triol, a gynura extract, a satureja montana flower / leaf extract and a buddleja globosa extract. The application adds the effective components of the conotoxin, the acetylated chitosan, the hydroxypropyl tetrahydropyran triol, the gynura extract, the satureja montana flower / leaf extract and the buddleja globosa extract on the basis of the moisturizing agent to prepare the eye composition with instant moisturizing, firming and anti-wrinkle effects. The skin horny layer moisture content improvement rate reaches 58.43-65.23%, the R2 value improvement rate reaches 9.43-13.25%, the F4 value reduction rate reaches 8.62-11.94%, the fish tail wrinkle length, depth and Ra value reduction rates are more than 22.68%, more than 5.62% and more than 16.52% respectively.
Owner:RENHE GLOBAL (SHANGHAI) GRAND HEALTH RESEARCH INSTITUTE CO LTD

Mu-type conotoxin peptide as well as pharmaceutical composition and application thereof

The invention discloses a mu-type conotoxin peptide as well as a pharmaceutical composition and application thereof. The amino acid sequence of the mu-type conotoxin peptide is shown as SEQ ID NO. 1. Compared with a wild type mu-CnIIIC, the mu-type conotoxin peptide [Ser17, Tyr6]-dR-mu-CnIIIC disclosed by the invention has the advantages that the animal activity is improved by more than 10 times, a Nav1.4 channel can be specifically blocked, muscle contraction is reduced, formation of wrinkles on the surface of human skin is reduced or eliminated, the mu-type conotoxin peptide [Ser17, Tyr6]-dR-mu-CnIIIC can also be used for relieving muscles and easing pain, and the mu-type conotoxin peptide [Ser17, Tyr6]-dR-mu-CnIIIC has a high-activity anesthesia effect.
Owner:PEPTIORIGIN BIOTECHNOLOGY CO LTD

A bicyclic peptide composition and its use in skin care

Disclosed are a bicyclic peptide composition and application thereof in skin care, and relate to the technical field of polypeptides, the composition comprising s-mu-conotoxin CnIIIC and a cyclic tetrapeptide-24 aminocyclohexane formate ester.The composition can be used for oil control, acne removal, repair, tightening, wrinkle reduction or anti-aging.
Owner:SHENZHEN WINKEY TECHNOLOGY CO LTD

Expression vectors for expression of recombinant u-conotoxin THIA or TIIIAlaMut in escherichia coli

PendingCN122459324AFusion Protein ExpressionNucleotide
The subject of this invention is a construct of an expression vector for expressing recombinant µ-conotoxin TIIIA or TIIIAlaMut, characterized in that it comprises the nucleotide sequence of µ-conotoxin TIIIA SEQ ID NO:1 or the nucleotide sequence of µ-conotoxin TIIIAlaMut SEQ ID NO:4, both sequences containing a sequence encoding six histidine residues (6His) at the 5' end, which is linked via a serine-glycine-serine linker (SGS) to a construct encoding a TRX::TIIIA fusion protein or a TRX::TIIIAlaMut fusion protein, wherein the TRX::TIIIA fusion protein comprises the µ-conotoxin TIIIA gene and a gene encoding a leader protein, and the TRX::TIIIAlaMut fusion protein comprises the µ-conotoxin TIIIAlaMut gene and a leader protein, wherein the leader protein is a thioredoxin (TRX) modified by site-directed mutagenesis, wherein the amino acid methionine at position 37 is replaced by lysine. Another subject of the invention is an expression vector comprising a construct according to the invention under the control of a constitutive promoter. Another subject of the invention is isolated *E. coli* cells comprising an expression vector according to the invention. Another subject of the invention is a method for producing µ-conotoxin TIIIA or TIIIAlaMut in *E. coli* using an expression vector comprising a construct according to the invention, characterized in that the method comprises the steps of: a) transforming *E. coli* cells with an expression vector comprising a construct according to the invention under the control of a constitutive promoter, said expression vector encoding a TRX::TIIIA fusion protein having the amino acid sequence SEQ ID NO:2 or having SEQ ID NO:2. a) TRX::TIIIAlaMut fusion protein NO:5; b) Expression of the TRX::TIIIA or TRX::TIIIAlaMut fusion protein; c) Isolation and purification of the TRX::TIIIA or TRX::TIIIAlaMut fusion protein; d) Formation of disulfide bonds by glutathione treatment of the purified TRX::TIIIA or TRX::TIIIAlaMut fusion protein in GSH / GSSG and dialyzing in buffer; e) Cleavage of the TRX::TIIIA or TRX::TIIIAlaMut fusion protein with the formed disulfide bonds by cyanogen bromide; f) Purification of the cleaved TIIIA or TIIIAlaMut peptide.
Owner:KEYAN BEAUTY CO LTD

α-conotoxin peptide lvid mutant, pharmaceutical composition comprising same, and use thereof

PCT designated stageWO2026007063A1Nervous disorderPeptide/protein ingredientsDiseaseConotoxin
Provided are an α-conotoxin peptide LvID mutant, a pharmaceutical composition comprising same, and a use thereof. Specifically, provided is an isolated polypeptide, which is a mutant of a polypeptide having an amino acid sequence as shown in SEQ ID NO: 1, and comprises the following mutations: E5A and Q11A. The isolated polypeptide can specifically block α7 nicotinic acetylcholine receptors (nAChRs), has high selectivity and strong blocking activity for the α7 nAChRs, and has the potential for preparing a drug for treating or preventing diseases related to the α7 nAChRs.
Owner:GUANGXI UNIV