126 results about "Cathelicidins" patented technology

The invention discloses cathelicidin-BF and a gene and application thereof, which belong to the field of biomedicine. The cathelicidin-BF is straight chain polypeptide and contains thirty amino acid residues, the molecular weight is 3,637.54Da, and the isoelectric point is 11.79. The complete sequence of the cathelicidin-BF is lysine-phenyl alanine-phenyl alanine-arginine-lysine-leucine- lysine-lysine-serine-valine-lysine-lysine-arginine-lactamine-lysine-glutamic acid-phenyl alanine- phenyl alanine-lysine-lysine-proline-arginine-valine-isoleucine-glycin-valine-serine-isoleucine- praline-phenyl alanine. The gene for encoding the cathelicidin-BF consists of 750 ribonucleotides, wherein 484th to 573rd ribonucleotides are used for encoding a mature peptide part. The cathelicidin-BF has small molecular weight, strong sterilization effect, and quick action time, and has quite strong killing function to a plurality of kinds of clinical drug-fast bacteria. In addition, the cathelicidin-BF also has the advantages of broad-spectrum antibiotics, salt independence and so on.

An endoluminal medical device comprises a drug release system that releases a cathepsin inhibitor at a predetermined location within a lumen of a patient. The endoluminal devices and methods of treatment of disease can treat illnesses such as aneurysms and aortic dissections.

The invention provides sequences of a snake venom cathelicidin antibacterial peptide consisting of non-natural fully D-type amino acid, which cannot be easily degraded by protease, and a derivative thereof and a preparation method thereof, and also provides application of the snake venom cathelicidin antibacterial peptide consisting of the non-natural fully D-type amino acid and the derivative thereof. The snake venom cathelicidin antibacterial peptide consisting of the non-natural fully D-type amino acid and the derivative thereof have an obvious effect of suppressing growth of bacteria and fungus, in particular to an excellent effect of suppressing clinical drug-resistant bacteria, have the beneficial characteristics of simple structure, convenience in artificial synthesis and wide antibacterial spectrum system, have the obvious characteristics of capability of resisting degradation of various protease, long antibacterial activity retention time and no drug residue, and can be applied to prevention and treatment of human or animal infected diseases, clinical artificial biomaterials, food preservative and fruit and vegetable refreshment, feed additives and daily chemical supplies.

The invention belongs to the technical field of biomedicine, and particularly relates to a transformed body antimicrobial peptide HC-15 of antimicrobial peptide Hc-CATH (cathelicidins) of hydrophis cyanocinctus and a preparation method and application of the transformed body. The transformed body antimicrobial peptide is the transformed body HC-15 of antimicrobial peptide Hc-CATH (cathelicidins) of hydrophis cyanocinctus, is linear chain polypeptide and comprises 15 amino acid residues, the tail end of C- is amidated, the molecular weight is 1974.46Da, and the isoelectric point is 12.61. The transformed body antimicrobial peptide HC-15 has high-potency antimicrobial activity; furthermore, the transformed body antimicrobial peptide HC-15 has beneficial characteristics of small molecular weight, simple structure, low hemolytic activity and simple preparation method.

Antimicrobial peptides and methods for their use are provided. The peptides are optimized, truncated versions of chicken cathelicidins (“fowlicidins”).

The invention relates to antimicrobial cathelicidin polypeptides related to a 38 amino acid peptide having SEQ ID NO:4. The invention provides for polypeptides having broad spectrum antimicrobial activity, nucleic acids and expression vectors encoding such polypeptides, as well as host cells and methods of reducing survival of a microbe. In addition, the invention also provides compositions, as well as articles of manufacture, that comprise a broad spectrum antimicrobial polypeptide.

The invention belongs to the technical field of biomedicine, and in particular relates to the application of cathelicidin-BF, an antibacterial peptide of ceratopsia, in the preparation of medicines for treating bacterial vaginosis. The antibacterial peptide cathelicidin-BF of the present invention has the beneficial characteristics of strong bactericidal effect and rapid sterilization on Staphylococcus aureus and Escherichia coli in vitro; the effect of cathelicidin-BF on vaginitis caused by E. The results of coccus-infected vaginitis are basically the same, and it can significantly inhibit Staphylococcus aureus or Escherichia coli in the vagina, and cathelicidin-BF has an obvious effect of reducing inflammation; it can be used in the preparation of drugs for treating bacterial vaginosis.

The invention relates to the field of biomedicine and in particular relates to an antibacterial polypeptide. Part of active amino acids of the antibacterial polypeptide of Cathelicidin family is mutated based on the antibacterial polypeptide of Cathelicidin family, and then the antibacterial polypeptide with high inhibitory activity to penicilin-resistant bacterium is obtained by solid phase chemical synthesis. The result of pharmacodynamic tests shows that the antibacterial polypeptide provided by the invention has good in vitro antibacterial activity and is applicable to treating diseases about drug-resistant bacterial infection.

The invention relates to an antimicrobial peptide Cm-CATH2, a preparation method thereof and an application. The Cm-CATH2 is a straight chain polypeptide containing 33 amino acid residues, the theoretical isoelectric point is 12.96, molecular weight is 4089.97Da, and net charge is +12. A gene of a precursor cathelicidin of the encoding antimicrobial peptide Cm-CATH2 comprises 486 nucleotides. The Cm-CATH2 has high antibacterial activity for Gram-negative bacteria, Gram-positive bacteria and fungi, comprises various clinical drug-resistant bacteria, is low in minimal inhibitory concentration and rapid and lasting in sterilizing effect, does not contain disulfide bonds and cyclic structures, has the advantages of low hemolysis, cell toxicity, difficulty in generating drug resistance and the like, can replace an antibiotic for preparing clinical drugs resisting pathogenic microorganism infection, diminishing inflammation and the like, is applied to additives in daily chemicals such as cosmetics, health care products, food and feed, and has an excellent application prospect. Chemical synthesis and gene engineering preparation are facilitated.

The invention relates to defensin cathelicidin-PP of polypedates puerensis as well as a gene and application thereof, and belongs to the field of biomedicine. The defensin cathelicidin-PP is a cyclic polypeptide encoded by a gene of defensin of Chinese amphibian polypedates puerensis, and has a molecular weight of 3,366.08 daltons and an isoelectric point of 10.05; the amino acid sequence of the defensin cathelicidin-PP is as shown by SEQ ID NO: 1. A gene GenBank Accession KY610282 for encoding a precursor of the defensin cathelicidin-PP of the polypedates puerensis consists of 615 nucleotide sequences; the nucleotide sequence of the gene GenBank Accession KY610282 is as shown by SEQ ID NO: 2, wherein nucleotides at No. 346 to No. 441 sites are encoding genes of defensin cathelicidin-PP of mature polypedates puerensis. The invention relates to the application of the defensin cathelicidin-PP of the polypedates puerensis to the preparation of a therapeutic medicine for infectious diseases caused by escherichia coli, salmonella paratyphi A, pseudomonas aeruginosa and candida glabrata. The defensin cathelicidin-PP has the obvious effects of inhibiting the growth of a bacterium and a fungus for the escherichia coli, the salmonella paratyphi A, the pseudomonas aeruginosa and the candida glabrata.

The invention discloses children antimicrobial peptides cathelicidins, a preparation method and the applications thereof. The nucleotide sequence and the amino acid sequence of children antimicrobial peptides Cathelicidin1, Cathelicidin2 and Cathelicidin3 are shown as a sequence table. The preparation method of the antimicrobial peptides adopts a solid-phase chemical synthesis method or a geneticengineering method. The genetic engineering method comprises the following steps of: respectively cloning the encoding genes of mature children antimicrobial peptides Cathelicidin1-3 to expression vectors; and then, guiding into host cells to express. By applying the genetic engineering technology in the invention, the children antimicrobial peptides Cathelicidins are expressed in the prokaryotichost cells with high efficiency. Proved by experiments, the antimicrobial peptides have obvious inhibition on various gram-positive bacteria and negative bacteria.

This invention relates to compounds of formula (I) which are cysteine protease inhibitors, in particular, inhibitors of cathepsins K, L, S and B. These compounds are useful for treating diseases in which inhibition of bone resorption is indicated, such as osteoporosis.

This invention relates to a novel class of compounds, represented by the formula (I) below, wherein the meanings of R1, R2, R3 and R4 are indicated therein, which are cysteine protease inhibitors, including but not limited to, inhibitors of cathepsins K, L, S and B. These compounds are useful for treating diseases in which inhibition of bone resorption is indicated, such as osteoporosis, osteoarthritis and rheumatoid arthritis.

The instant invention is drawn to methods useful for the treatment or the prevention of a viral infection. The methods include administering at least one compound that is an inhibitor of cathepsin L to an individual. The methods are particularly useful in individuals infected with, or at risk of infection with, SARS virus or Ebola virus. The invention also includes methods of identifying potential therapeutics for use in the methods of treatment or prevention of a viral infection.

Agents and natural and synthetic formulations and extracts are useful in control of pathogen infection and infestation in humans, animals and plants, as well as pathogen contamination in environmental locales. A method inhibits growth or infection or infestation of a pathogen, including contacting the pathogen with an effective amount of a combination of a plant defensin or a functional natural or synthetic derivative or variant thereof and a non-defensin peptide, such as a cathelicidin peptide, a hairpin peptide, a hairpin peptide from which disulfide bridges have been removed, indolicidin, synthetic peptide CP-29, or a peptide derived from a cystatin. The combination of the defensin and peptide are synergistic compared to the use of each alone at the same individual dose as used in the combination.

The present invention provides a compound of the Formula:

a pharmaceutically acceptable salt, a solvate, or a prodrug thereof, wherein m, n, Ar¹, R¹, R², R³, R⁴, and R⁵ are those defined herein. The present invention also provides methods for using and preparing compounds of Formula I.

The invention relates to an antimicrobial peptide Ea-CATH1 of Equus asinus and genes and applications thereof, belonging to the technical field of biological medicine. Ea-CATH1 is one genetic coding straight-chain polypeptide of Cathelicidin of Equus asinus, and the complete sequence of Ea-CATH1 is as follows: lysine-arginine-arginine-glycin-serine-valine-threonine-threonine-arginine-tyrosine-glutamine-phenylalanine-leucine-methionine-isoleucine-histidine-leucine-leucine-arginine-proline-lysine-lysine-leucine-phenylalanine-alanine. The gene coding Ea-CATH1 precursor is composed of 550 nucleotides and the part coding mature peptide is the 391-465th nucleotides. Ea-CATH1 has smaller molecular weight, stronger bactericidal effect and broader spectrum and extremely strong killing effect on various clinical drug-resistance bacteria; Ea-CATH1 has simple structure, does not contain disulfide bond and ring structure and is suitable to be prepared by chemical synthesis and gene engineering; and Ea-CATH1 also has useful characteristics such as no hemolysis and ultrastrong serum stability.

Cationic antimicrobial peptides (AMPs) are an integral part of the innate immune system. Cathelicidin and defensin homologs from a variety of species exhibit broad-range bactericidal activity. The human cathelicidin analog, hCAP18, is encoded by the CAMP gene. Vitamin D3 and its analogs upregulate transcription of CAMP and defensin B2 (defB2) genes, leading to increased expression of hCAP18 mRNA and defB2. Induction of CAMP was observed in acute myeloid leukemia (AML), immortalized keratinocyte and colon cancer cell lines, as well as normal human bone marrow (BM)-derived macrophages and fresh BM cells. The present invention provides methods of inducing cathelicidin production by administering Vitamin D3 or Vitamin D3 analogs, as well as methods of treating skin infections and infections of the colon, sepsis and wound healing, preventing bacterial growth on skin grafts, promoting angiogenesis, and promoting chemoattraction by administering Vitamin D3 or Vitamin D3 analogs to upregulate cathelicidin and defensin expression.