45results about How to "Low hemolytic toxicity" patented technology

The invention discloses a micromolecule synthesized anti-microbial peptide, as well as a preparation method and application thereof. The sequence of a cationic anti-microbial peptide is SQ1: R-W-W-R-F-NH2 (Arg-Arg-Trp-Trp-Arg-NH2), and the preparation method is the solid-phase chemosynthesis method. The micromolecule synthesized anti-microbial peptide has broad-spectrum cytotoxicity to gram-positive bacteria and gram-negative bacteria, has stronger bactericidal activity than a natural anti-microbial peptide, is simple in structure, convenient for artificial synthesis without any modification and connection, has the advantages of small hemolytic toxicity and no poison effects on animal and plant cells, and has an important value in development and application of antimicrobial agents.

The invention discloses a pillar[5]arene artificial transmembrane channel having an antibacterial activity, and a production method and an application thereof, and belongs to the technical field of compounds having an antibacterial activity. The structural general formula of the pillar[5]arene artificial transmembrane channel having the antibacterial activity is shown in the description. The invention also discloses the production method of the pillar[5]arene artificial transmembrane channel having the antibacterial activity, and an application of the pillar[5]arene artificial transmembrane channel in the preparation of medicines for treating or preventing bacterium induced diseases. The artificial transmembrane channel produced in the invention has an excellent antibacterial performance,so the artificial transmembrane channel can be well applied to the prevention and treatment of bacterium induced animal and plant diseases; and the produced artificial transmembrane channel has very low hemolysis toxicity, so the artificial transmembrane channel can be used as a whole-body ion channel type antibiotic candidate medicine.

The invention provides enzymolysis-resisting antibacterial peptide I9H12 as well as a preparation method and application thereof. A sequence of the antibacterial peptide I9H12 is shown as SEQ ID No. 1in a sequence table. The preparation method comprises the following steps: referring to the properties of amino acids; meanwhile, avoiding enzyme digestion sites of main proteinase in a body as muchas possible, and selecting hydrophobic amino acid isoleucine (Ile) and positive-charge amino acid histidine (His) as main amino acids to newly design the antibacterial peptide I9H12; carrying out amidation on a carboxyl terminal of the peptide to improve one positive charge and increase the stability of the peptide. The invention also provides the application of the antibacterial peptide to the preparation of targeting antibacterial medicines for treating gram-negative bacterium or fungus infectious diseases. According to the enzymolysis-resisting antibacterial peptide I9H12, the enzymolysis-resisting capability of the antibacterial peptide is effectively improved, and the application potential in actual production is improved.

The invention relates to a cyclic peptide with antiviral, antibacterial and antifungal activity. The cyclic peptide has an amino acid residue sequence Cyclo (CGESCVFIPCITTVLGCSCSIKVCYKNGSIP) shown in SEQ ID NO:1, wherein three pairs of disulfide bonds are respectively formed by Cys in the first and the 17th sites, Cys in the fifth site and the 19th site and Cys in the 10th site and the 24th site, so that the cyclic peptide has thermotropy resistance and proteaseenzymolysis stability, and is low in hemolytic toxicity. Therefore, a pharmaceutical composition containing the cyclic peptide or salts thereof can be used for preventing or treating the diseases such as influenza viruses A, bacteria and fungi of people or livestock.

The invention belongs to the technical field of medicines, in particular relates to a novel alpha-hederin derivative and a preparation method and use thereof, and more particularly relates to a novel alpha-hederin derivative shown in general formula (I) and a preparation method and anti tumor use thereof. Compared with alpha-hederin, the novel alpha-hederin derivative has significant cytotoxicity, hemolytic toxicity is greatly reduced, and the novel alpha-hederin derivative has certain antitumor activity on a tumor-bearing mice model, and can be used for preparing anti-tumor drugs or tumor adjuvant treatment drugs.

The invention discloses an antimicrobial hexapeptide. The antimicrobial hexapeptide has a sequence of Arg-Arg-Trp-Trp-Arg-Trp. The antimicrobial hexapeptide can be used in preparation of drugs for treating or preventing bacterial infection. The invention also provides an antimicrobial hexapeptide derivative. The antimicrobial hexapeptide derivative has a sequence of Arg-Arg-Trp-Trp-Arg-Trp-beta-phenylethylamine. The antimicrobial hexapeptide derivative can be used in preparation of drugs for treating or preventing bacterial infection. The bacterium is drug-resistant acinetobacter baumannii. The artificially designed synthetic antimicrobial hexapeptide and its phenylethylamine-modified product can be conveniently obtained by a solid phase synthesis method. The synthetic antimicrobial peptide and its derivative have broad spectrum killing activity to Gram-positive bacteria and Gram-negative bacteria, and particularly, the derivative exhibits stronger antibacterial activity to drug-resistant acinetobacter baumannii, has very small hemolytic toxicity and can be used in drugs for treatment or prevention of diseases caused by drug-resistant acinetobacter baumannii.

The invention provides an anti-enzymolysis branched antibacterial peptide Pal-CRKP as well as a preparation method and application of the anti-enzymolysis branched antibacterial peptide Pal-CRKP. The amino acid sequence of the branched antibacterial peptide Pal-CRKP is as follows: Pal-GGGK (CRKPCRKP) CRKPCRKP, and Pal is n-hexadecanoic acid. According to the preparation method, by utilizing the characteristics of a lysine side chain, n-hexadecanoic acid and an anti-enzymolysis peptide sequence unit are combined by utilizing lysine to form a branched antibacterial macromolecule, and the branched antibacterial peptide with high antibacterial activity, low toxicity and high stability is designed. The anti-enzymolysis branched antibacterial peptide Pal-CRKP not only shows high-efficiency bacteriostatic activity on gram-negative bacteria, but also has a high-efficiency inhibition effect on gram-positive bacteria, meanwhile, the anti-enzymolysis branched antibacterial peptide Pal-CRKP has relatively low hemolytic toxicity, and the degradation degree of high-concentration protease on the branched antibacterial peptide Pal-CRKP is very weak, so that the anti-enzymolysis branched antibacterial peptide Pal-CRKP can be used for preparing the anti-enzymolysis branched antibacterial peptide Pal-CRKP. The anti-enzymolysis branched antibacterial peptide disclosed by the invention has relatively high development potential of replacing antibiotics.

The invention relates to a novel recombinant bee venom polypeptide of which an amino acid sequence is SEQ ID No.1. A nucleotide sequence for encoding a novel recombinant bee venom protein is SEQ ID No.2. The preparation method comprises the steps: connecting a UA8 oligopeptide and a melittin gene to form a recombinant bee venom fusion gene, an eukaryotic expression vector U-melittin-pPICZalpha ofthe recombinant bee venom fusion gene is constructed, and pichia pastoris is transferred to carry out induced expression of the recombinant bee venom protein and also carry out expression and purification. The novel recombinant bee venom polypeptide has stronger antitumor activity and lower hemolytic toxicity than a melittin and is applied to the prevention and treatment of cervical cancer causedby an HPV virus.

The invention provides a hornet phallotoxin antitone analog WVD-II and a preparation method and application thereof, and belongs to and relates to the technical field of polypeptide synthesis. The amino acid sequence of the hornet phallotoxin antitone analog WVD-II is as shown in SEQID NO:1. The N end of the hornet phallotoxin antitone analog WVD-II disclosed by the invention has positive charges,so that the N end can be combined with a cell membrane having negative electricity; an alpha helical structure is formed from hydrophobic amino acids at a C end, and can bore a hole in the surface ofthe cell membrane, so that death of bacteria is caused. The in vitro antibacterial activity determination indicates that the hornet phallotoxin antitone analog WVD-II disclosed by the invention has significant sterilizing effects on gram-positive bacteria, gram-negative bacteria and fungi, has good stability, is low in hemolytic toxicity and has the characteristics of being broad-spectrum, efficient and safe. The hornet phallotoxin antitone analog WVD-II disclosed by the invention can be used as an active component clinically for replacing traditional antibiotics for treatment.

The invention discloses cationic antibacterial peptide as well as a preparation method and application thereof. The sequence of the cationic antibacterial peptide is as follows: SK1:FRWWR-NH2((Phe-Arg-Trp-Trp-Arg-NH2); the preparation method is a solid phase chemical synthesis method. the cationic antibacterial peptide provided by the invention has broad-spectrum killing activity to gram-positive bacteria and gram-negative bacteria and has higher bactericidal activity when being compared with natural antibacterial peptide; besides, the cationic antibacterial peptide has the advantages that the structure is simple, artificial synthesis is convenient, no decorative connection is required, the hemolytic toxicity is small, and no toxic effect is caused to animal and plant cells; the cationic antibacterial peptide has very important values in the aspects of development and application of antibacterial medicines.

The invention provides a palmitic anti-enzymolysis antibacterial peptide, and a preparation method and application thereof. The sequence of the antibacterial peptide B3C16 is C16-GGGK(PRPR)K(PRPR)RPRP, wherein C16 is palmitic acid. The side chain of each lysine is linked with a polypeptide branched chain PRPR through an amide bond to form steric hindrance between a dendritic structure and a peptide chain; further, palmitic acid is used as a main hydrophobic source of the antibacterial peptide sequence, so that hydrolysis of hydrophobic amino acids by all proteases is perfectly avoided; and finally a flexible amino acid connector GGG is used for linking the palmitic acid with a branched peptide to form a perfect amphiphilic structure. The antibacterial peptide has high-efficiency inhibitioneffect on standard bacteria and drug-resistant bacteria such as Gram-negative bacteria, Gram-positive bacteria and the like, and has very low hemolytic toxicity, and the hydrolysis degree of high-concentration protease to the B3C16 is low.

The invention belongs to the technical field of medicinal chemistry, and discloses a tri-cationic quaternary ammonium salt antibacterial peptide simulant with antibacterial activity and a preparation method thereof. The compounds have the following structural general formulas I-III. In-vitro antibacterial activity experiments prove that a part of the series of compounds show good activity on gram-positive bacteria staphylococcus aureus and enterococcus faecalis and gram-negative bacteria escherichia coli and stenotrophomonas maltophilia, and the compounds have excellent broad-spectrum antibacterial activity; meanwhile, in-vitro red blood cell hemolytic data show that the compound is relatively low in hemolytic toxicity and relatively good in selectivity.

The present invention addresses the problem of providing an antithrombotic metallic material which has improved safety against low hemolytic toxicity and can exhibit high antithrombotic properties sustainably. The present invention provides an antithrombotic metallic material comprising a metallic material of which the surface is coated with a coating material, wherein the coating material comprises a phosphonic acid derivative or a catechol derivative, a polymer containing, as a constituent monomer, a compound selected from the group consisting of an alkyleneimine, vinylamine, allylamine, lysine, protamine and diallyl dimethyl ammonium chloride and a sulfur-atom-containing compound having an anionic anticoagulant activity, the polymer is covalently bonded to the phosphonic acid derivative or the catechol derivative, the phosphonic acid derivative or the catechol derivative is bonded to the metallic material through a phosphonic acid group or a catechol group contained in the derivative, and the ratio of the amount of nitrogen atoms to the total amount of all of atoms is 4.0 to 13.0% by atom number when the surface of the antithrombotic metallic material is measured by an X-ray photoelectron spectroscopy (XPS).