38results about How to "Simple experimental technique" patented technology

The invention provides a preparation method of indium oxide with new appearance, belonging to the technical field of synthesis and nano material of the indium oxide. The preparation method comprises the following steps: taking inorganic salt solution of the indium as an indium source, adopting N, N-dimethyl formamide (DMF) as an alkali source and anion active agents such as sodium dodecyl sulfate(SDS) and the like as an additive, using hydrothermal synthesis to prepare the novel hollow-microspherical and flower-shaped indium oxide with the secondary structure under the condition without adding any hard template, and controlling the appearance of the secondary structure by chemical means. In the preparation method provided by the invention, the technical process is simple, the promotion is easy, the selected reagent is low in price and environment-friendly, and the need on low-cost, large-scale and green production is met.

The invention provides a derived peptide IR2 of a pig-derived antibacterial peptide as well as a preparation method and application thereof. The sequence of the derived peptide IR2 of the pig-derived antibacterial peptide is as shown in SEQ ID No.1. Antibacterial peptides IR1 and IR2 are obtained by using a fixed point amino acid fragment interception and binary amino acid sequence superimposing method for intercepting six amino acid fragments of a pig-derived PG-1 corner part and symmetrically and circularly arranging charged amino acid arginine and hydrophobic amino acid isoleucine serving as repeated binary sequence units at the two sides of the corner. The antibacterial activity of the antibacterial peptide IR2 is higher than that of the antibacterial peptide IR1. The therapeutic index of the antibacterial peptide IR2 reaches up to 43.2 and is 216 times of that of the pig-derived antibacterial peptide RG-1. By virtue of the method, the hemolytic activity of the antibacterial peptide is greatly reduced under the condition of increasing the antibacterial activity of the antibacterial peptide, the selectivity of the antibacterial peptide between bacterial cells and mammalian cells is increased, and the development potential of the antibacterial peptide serving as antibiotic substitutes is improved.

The invention provides a multi-stranded beta-hairpin short-peptide with tolerant protease and a preparation method and an application. A sequence is as shown in a SEQ ID No.1. The short-peptide provided by the invention fully exerts the structural advantages of a beta-hairpin structure to obtain a multi-stranded beta-hairpin structural antibacterial peptide. The stability is further improved while the activity is ensured by using a common amino, and composition of a corner amino acid is changed, so that a series of multi-stranded beta-hairpin antibacterial peptides of brand new structures: (WRXxRW)n-NH2, wherein n is 1, 2, 3 and 4; PG is selected as a corner to describe; when n is equal to 2, the antibacterial peptide is named W2; and when n is equal to 3, the antibacterial peptide is named W3. The peptide verifies relatively high cell selectivity and salt ion tolerance, and moreover, based on the activity of the antibacterial peptide with structural stability, the obtained antibacterial peptide is also relatively short, and relatively strong tolerance of in vivo protease is also represented.

The invention provides a tryptophan tension chain-beta-hairpin antibacterial peptide and a preparation method and application thereof. A sequence of the antibacterial peptide is as shown in a sequence table SEQ ID No.1. The preparation method comprises the following steps: by taking a tryptophan tension chain structure as a template, combining amino acid composition and structural characteristics of the antibacterial peptide; and by using interaction of cross-chain W-W as a structural stable factor, symmetrically and circularly arranging an amino acid lysine with charges and a hydrophobic amino acid tryptophan as repeated binary sequence units on two arms of the beta-hairpin to obtain the antibacterial peptide WK3. The antibacterial peptide has relatively high bacteriostatic activity and cell selectivity, and the treatment index reaches up to 161.27. The antibacterial peptide designed by the method needs not to bind a disulfide bond but has extremely high structural stability, so that the selectivity of the antibacterial peptide between bacterial cells and mammalian cells is improved, and the antibacterial peptide has an application potential as an antibiotic substituent. The antibacterial peptide is relatively high in activity and relatively low in cytotoxicity.

The invention discloses an improved mitochondrial genome complete sequence determination method based on the conventional PCR technology, which aims at providing a low-cost, fast and new mitochondrial genome complete sequence determination method having a simple experimental technology. The method is characterized by the screening of templates and the design of PCR primers, i.e determining the minimal homology of mitochondrion complete sequences of closely-related species which can be used as the templates; carrying out primer design in two batches, and introducing a nested-PCR method to the sequence amplification process; and presenting general rules for the design of the PCR primers. The method is mainly used for mitochondrial genome complete sequence determination, and serves basic scientific researches, such as genetics, molecular biology and the like.

The invention relates to an antibacterial peptide GW13 and its preparation method and use. The antibacterial peptide GW13 has an amino acid sequence of GlyLeuArgProLysTyrSer(ArgTrpLeu)2-NH2. The preparation method comprises the following steps of 1, cutting out 13 amino acid fragments from a linear chicken beta-defensin 4 carboxyl end by a fixed-point amino acid fragment cutting method, removing disulfide bonds to obtain a GW10 (GlyLeuArgProLysTyrSerArgTrpLeu-NH2) fragment, and repeating connecting characteristic three-residue complexes ArgTrpLeu to obtain the antibacterial peptide GW13, and 2, synthesizing a peptide resin in a polypeptide synthesizer by a solid-phase synthesis method, carrying out TFA cutting to obtain a polypeptide, and carrying out reversed-phase high-performance liquid chromatography purification. The antibacterial peptide GW13 obtained by the preparation method has strong bacteriostatic activity, low hemolytic activity, the highest therapeutic index and a large development potential.

The invention relates to an efficient alpha-helix antibacterial peptide GV and a preparation method and application thereof. The antibacterial peptide GV is an antibacterial peptide with high cell selectivity and achieves an optimal point of junction of the antibacterial activity and cell toxicity of the antibacterial peptide. A sequence of the antibacterial peptide GV is represented by a sequence table SEQ ID No. 1. The preparation method comprises the following steps: (1) carrying out designing in accordance with alpha-helix peptide GRX2RX3RX2RG serves as a template, so as to obtain a brand-new antibacterial peptide GV, wherein X= V; (2) synthesizing a polypeptide crude product through a polypeptide synthesizer by a solid-phase chemical synthesis method; purifying the synthesized polypeptide by using out-phase high-performance liquid chromatography, and carrying out identification on the synthesized polypeptide by using electrospray mass spectrography, thereby preparing the polypeptide. The antibacterial peptide GV provided by the invention has relatively high bacteriostatic activity and relatively low hemolytic activity and is the highest in therapeutic index, thereby having great development potential.

The invention provides a derived peptide for a chicken origin antibacterial peptide as well as a preparation method and application thereof. The sequence of the derived peptide is shown as SEQ No.1. The preparation method comprises the following steps: intercepting 20 amino acids of a chicken origin AvBD4 leader peptide, replacing 5th cysteine and 6th, 7th and 12th phenylalanine by amino acid lysine with charges respectively, meanwhile, carrying out amidation on a carboxyl terminal of the antibacterial peptide, and increasing a positive charge to improve the stability of the antibacterial peptide; adopting a solid-phase chemical synthesis method to obtain crude MGW21; and purifying and identifying synthesized polypeptide by using reversed-phase high performance liquid chromatography and electrospray mass spectrometry. The invention provides the application of the antibacterial peptide in preparing a medicament for treating gram-positive bacteria or gram-negative bacteria infectious diseases. The antibacterial peptide is good in amphiphilic property; compared with an antibiotic and Melittin, the antibacterial peptide is high in antibacterial activity and low in cytotoxicity.

The invention provides an imperfect amphiphilic antimicrobial peptide PRW4-R and a preparation method and application thereof. The sequence of the imperfect amphiphilic antimicrobial peptide PRW4-R is shown as SEQ ID No. 1. The preparation method comprises the following steps: cutting out 16 amino acid sequences at a PMAP-36N end to obtain RI16 with a perfect amphiphilic structure; based on an Alpha-helix protein folding principle, substituting Trp for paired Lys in the polar face of the amphiphilic structure to obtain imperfect amphiphilic antimicrobial peptide PRW4; and substituting Arg for all lysine in the sequence of the PRW4 to obtain the PRW4-R. The therapeutic index of the PRW4-R is up to 161.5; and the peptide PRW4-R shows high cell selectivity and has low hemolytic activity, so that the development potential of the peptide PRW4-R in becoming a substituent of antibiotics is improved.

The invention relates to the technical field of preparation of transition metal carbides, in particular to a preparation method of spherical carbon-coated nickel with different carbon layers and a hydrogen evolution property for water electrolysis of the spherical carbon-coated nickel. The preparation method comprises the following steps: (1) uniformly dispersing nickel nitrate hexahydrate and glycine in anhydrous ethanol by mechanical stirring; (2) transferring the mixed liquid to a reaction kettle, and carrying out a reaction for 12 hours at the temperature of 180 DEG C to obtain a carbon-coated nickel precursor; and (3) conducting roasting in nitrogen under a certain temperature condition to obtain the spherical carbon-coated nickel composite materials respectively. The method has the advantages that the raw materials are cheap and easy to obtain, synthesis is facilitated, equipment is simple, the production process is pollution-free, large-scale production can be quickly realized,and the material has lots of active sites and good hydrogen evolution properties for water electrolysis.

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 discloses a targeting antimicrobial peptide and a preparation method and application thereof. A sequence of the targeting antimicrobial peptide cCF10-C4 is shown in a sequence table SEQ ID No.1. The preparation method comprises the steps that enterococcus faecalis serves as a target bacterium to obtain the targeting antimicrobial peptide cCF10-C4 through design, a series of multi-structural-domain antimicrobial peptide molecules having selectivity to the enterococcus faecalis are established in a heterozygous mode. The design of a series of antimicrobial peptide molecules mainly includes two independent functional areas, namely a sterilization area and an identification area respectively. The targeting antimicrobial peptide has targeting selection capability to the target bacterium. The targeting antimicrobial peptide cCF10-C4 is conductive to reestablishment of microecological balance after treatment.

The invention discloses a kit for rapidly detecting the SNP site of a Y chromosome and a method, and the method is applied to the rapid identification of Y chromosome haplotype pedigrees of male individuals in forensic science. The rapid detection kit for the identification of the characteristic sites of the Y chromosome haplotype pedigrees of East Asian males includes primers corresponding to theSNP characteristic sites used for amplification detection of the Y chromosomes and probes of two mutation type sequence characteristics representing the SNP sites. The using method includes adding asample into plates having 96 or 384 pores, and performing an amplification reaction in a PCR instrument after a PCR reaction system is well mixed; putting the plates into the quantitative PCR instrument having an SDS scanning function to read a fluorescence signal after the amplification is finished; and automatically analyzing the Y-SNP haplotype of the sample by the instrument according to the fluorescence signal, and outputting a result in a spreadsheet. Through the kit, the detection can be completed by one step amplification, purification and template preparation are not needed, and the detection process of the Y-SNP can be simplified.

The invention relates to efficient hybrid antibacterial peptide LI and a preparation method and application thereof. A sequence of the efficient hybrid antibacterial peptide LI is shown as SEQ ID No.1 of a sequence table. The preparation method includes following steps: according to a fixed-point amino acid fragment intercepting method, intercepting an amino acid residue fragment from the 14th locus to the 21st locus of human-derived antibacterial peptide LL37 and an amino acid residue fragment from the 5th locus to the 13th locus of bovine-derived antibacterial Indolicidin, and sequentially connecting the two fragments to obtain the antibacterial peptide LI; 2), using a polypeptide synthesizer for solid-phase synthesis to synthesize peptide resin; obtaining polypeptide after TFA cutting, and adopting reverse-phase high-performance liquid chromatography for purifying. The antibacterial peptide LI obtained by the method has high antibacterial activity, weak hemolytic activity, high treatment index and huge development potential.

The invention discloses a preparation method and application of a beta-phase ferronickel hydroxide/carbon nanotube compound with atomic defects, and the preparation method comprises the following steps: (1) uniformly dispersing carbon oxide nanotubes in deionized water (introduced with nitrogen) by adopting an ultrasonic dispersion technology; (2) adding nickel chloride hexahydrate, ferrous chloride tetrahydrate, hexamethylenetetramine and ammonium fluoride into the solution, transferring into a reaction kettle, and reacting at 120 DEG C for 6 hours to obtain a ferronickel hydroxide/carbon nanotube compound; and (3) dispersing the obtained material in a mixed solution of hydrogen peroxide and water at room temperature to oxidize ferronickel hydroxide/carbon nanotube compounds with different defect degrees for different time. The method has the advantages of cheap and accessible raw materials, convenient synthesis, simple equipment and no pollution in the production process, can quicklyimplement large-scale production, and has the advantages of more defect sites, more active centers and favorable water electrolysis and oxygen evolution properties.

The invention provides a high cell-selectivity cyclic antimicrobial peptide OIR3 and a preparation method and application thereof. The high cell-selectivity cyclic antimicrobial peptide OIR3 has a sequence shown in the formula of SEQ ID No. 1 in the sequence table. The preparation method comprises 1) designing a cyclic antimicrobial peptide OIR3 according to a cyclic antimicrobial peptide template (IleArg)nPro(IleArg)n, wherein n is 3, and 2) synthesizing a peptide resin by a solid phase synthesis method using a polypeptide synthesizer, carrying out TFA cutting to obtain a polypeptide, and carrying out reversed-phase high-performance liquid chromatography purification so that the antimicrobial peptide OIR3 is obtained. The antimicrobial peptide can be used in drugs for treating diseases infected by gram-positive bacteria or gram-negative bacteria. The antimicrobial peptide OIR3 is a high cell-selectivity cyclic antimicrobial peptide, has strong antibacterial activity and weak hemolytic activity, has the highest treatment index and has a great development potential.