16results about How to "Low hemolytic activity" patented technology

The invention discloses application of a low-toxicity broad-spectrum antibacterial peptide taking WW as a symmetric center, WK is repeated twice and symmetrically distributed on two sides, WW is taken as the symmetric center to obtain an antibacterial peptide WKWKWWKWKW-NH2 (N2W2), and tryptophan at the C terminal and the N terminal of the N2W2 is replaced with leucine and / or isoleucine to obtain the antibacterial peptide. The antibacterial peptide can basically maintain the excellent antibacterial activity of the parent peptide, and the hemolytic activity of the antibacterial peptide is greatly reduced, so that the safety is improved. Wherein the antibacterial activity of IL-N2W2 is the highest, but the stability of IL-N2W2 needs to be improved, so that D-IL-N2W2 is obtained by carrying out D-type amino acid substitution on IL-N2W2. The D-IL-N2W2 keeps the high antibacterial activity and low toxicity of IL-N2W2, can still completely inhibit the growth of bacteria after being incubated with high-concentration trypsin or chymotrypsin, has great potential in the aspect of relieving the drug resistance of antibiotics, and has good application prospects in preparation of clinical antibacterial drugs.

The invention is applicable to the technical field of polypeptides, and provides a novel antibacterial peptide GG25 and application thereof, and the amino acid sequence of the antibacterial peptide GG25 is as shown in SEQ ID No.1. The molecular weight of the novel antibacterial peptide GG25 is 2890.52 Da, and the novel antibacterial peptide GG25 has antibacterial activity on escherichia coli, klebsiella pneumoniae, pseudomonas aeruginosa, enterococcus faecalis, salmonella typhimurium, methicillin-resistant staphylococcus aureus, staphylococcus aureus, staphylococcus epidermidis, listeria monocytogenes and bacillus subtilis; the hemolytic activity is low, the cytotoxicity is small, and the escherichia coli and methicillin-resistant staphylococcus aureus are not easily induced to generate drug resistance; in addition, the gelatin chitosan food coating containing GG25 also has a good beef preservation effect, and can be applied to the fields of food, animal husbandry, medicine and the like.

The invention discloses a phenanthro [9, 10-d] imidazole quaternary ammonium salt derivative as well as preparation and antibacterial application thereof. According to the series of compounds, phenanthro [9, 10-d] imidazole quaternary ammonium salt derivatives which are novel in structure and good in antibacterial activity are prepared by taking phenanthro quinone as a lead compound and modifying the structure of phenanthro quinone, the structural general formula of the phenanthro [9, 10-d] imidazole quaternary ammonium salt derivatives is shown in the specification, and R is selected from H, C6-C14 alkyl or C3-C8 alkylene. The phenanthro [9, 10-d] imidazole quaternary ammonium salt derivative prepared by the invention has a relatively good antibacterial effect on gram-positive bacteria such as staphylococcus aureus S.aureus ATCC 29213 and various clinical methicillin-resistant staphylococcus aureus (MRSA), meanwhile, the water solubility is improved, the biotoxicity of a parent body is reduced, and the phenanthro [9, 10-d] imidazole quaternary ammonium salt derivative has relatively high yield and is suitable for industrial production. The compound is expected to be further developed into a clinical candidate antibacterial drug. # imgabs0 #

The invention discloses a wood frog antibacterial peptide and application thereof in antibiosis, anti-inflammation and antioxidation, and belongs to the technical field of biology. The method comprises the following steps: firstly, analyzing skin mucus of wood frogs in Northeast by utilizing a peptidomics technology to obtain a large amount of peptide fragment information; and then, comparing the peptide fragment information with a known antibacterial peptide database, and screening out peptide fragments which possibly have antibacterial activity. Furthermore, through experiments, an antibacterial peptide which is extremely low in hemolytic activity and highly stable to pH and temperature and has anti-inflammatory and anti-oxidation effects is screened out. The amino acid sequence of the antibacterial peptide is as shown in SEQ ID NO: 3, and the antibacterial peptide lays a foundation for enriching the types of antibacterial peptides and adds new advantages for the application of the antibacterial peptide.

This invention belongs to the field of antimicrobial peptide technology, and particularly relates to a broad-spectrum antimicrobial peptide with low hemolytic activity and its applications, as well as a broad-spectrum antibacterial drug. The antimicrobial peptide is named AY6, and its amino acid sequence is shown in SEQ ID NO.1. Antimicrobial peptide AY6 exhibits significant antibacterial effects against both Gram-positive and Gram-negative bacteria, with a bactericidal rate far exceeding that of traditional antibiotics, enabling highly effective responses to bacterial infections. AY6 has low hemolytic activity and good biocompatibility, making it suitable for medical anti-infective applications. The antimicrobial peptide provided in this application has a short sequence, is easy to synthesize chemically, can save on large-scale production costs, and has broad application prospects.

The invention provides a beta-hairpin antibacterial peptide based on Trp-label cross-chain interaction as well as a preparation method and application of the beta-hairpin antibacterial peptide based on Trp-label cross-chain interaction. A beta-hairpin antibacterial peptide WRFPG is used as a basis, the amino acid sequence of the beta-hairpin antibacterial peptide WRFPG is shown as SEQ ID No.2, five polypeptides are obtained and synthesized through a solid-phase chemical synthesis method, the antibacterial peptide with excellent antibacterial activity and low toxicity is screened out through determination of antibacterial activity and determination of hemolytic activity and cytotoxicity, the amino acid sequence of the antibacterial peptide is shown as SEQ ID No.1, the C end of the antibacterial peptide is amidated by-NH2, and the amino acid sequence of the antibacterial peptide is shown as SEQ ID No.1. The antibacterial peptide is finally named as the antibacterial peptide KKRRPG. According to the antibacterial peptide KKRRPG disclosed by the invention, the antibacterial activity is ensured, the hemolytic activity is reduced, and the selection index of human embryo kidney cells HEK293t is improved.

The application provides a preparation of gramicidin and an antibacterial hydrogel preparation of the gramicidin, and discloses medical uses of the gramicidin, and provides a recombinant gramicidin, heterologous expression of the gramicidin is realized by constructing a Pichia pastoris recombinant strain, and the antibacterial activity of the gramicidin is retained, and the method has the advantages of simplicity and rapidness. Meanwhile, the hydrogel preparation of the gramicidin provided by the application shows good potential for treating wound infection of a diabetic mouse, and has the performance of rapid adhesion and hemostasis, lays a foundation for development of a new antibacterial drug, and provides a new direction for treatment of chronic inflammatory wounds and open bleeding.

The invention provides a targeting antibacterial peptide HI-WK targeting escherichia coli K88 as well as a preparation method and application of the targeting antibacterial peptide HI-WK, and belongs to the technical field of biology, and the sequence of the targeting antibacterial peptide HI-WK is shown as SEQ ID No.1. A peptide fragment HI with escherichia coli affinity is obtained through screening of a phage display heptapeptide library, an active peptide WK is added on the basis of an affinity sequence, the sequence of the active peptide WK is shown as SEQ ID No.3, and the active peptide WK is used for improving penetrability to escherichia coli cell membranes, so that the antibacterial peptide HI-WK is obtained. Biological safety detection shows that the minimum inhibitory concentration of the antibacterial peptide HI-WK on escherichia coli K88 is increased by 2 times compared with that of the active peptide WK, and the geometric average of the minimum inhibitory concentration of the antibacterial peptide HI-WK on other escherichia coli is reduced by 1.78 times. In addition, the antibacterial peptide HI-WK does not show hemolytic activity when the concentration is 128 [mu] M, and the antibacterial peptide HI-WK has high application value.

The invention discloses an anti-enzymolysis antibacterial peptide FRL as well as a preparation method and application thereof, and belongs to the field of bioengineering, and the sequence of the antibacterial peptide FRL is as shown in SEQ ID No.1. The antibacterial peptide FRL shows a narrow-spectrum antibacterial effect, can effectively inhibit gram-negative bacteria, and has the potential of being applied to drugs for treating gram-negative bacteria infectious diseases. The antibacterial peptide has very low hemolytic activity and eukaryotic cell toxicity. The antibacterial peptide cannot cause 10% red blood cell hemolysis under the concentration of 128 [mu] mol / L, and the survival rate of mouse macrophages RAW264.7 reaches 80% or above. The antibacterial peptide can be used for treating trypsin, pepsin, chymotrypsin and protease K (0.4 mg / mL) under the conditions that the pH is equal to 5 and the temperature is 37 DEG C; 0.5 h), good stability is shown. In conclusion, the antibacterial peptide FRL has the development potential of becoming an antibiotic substitute.

This invention discloses broad-spectrum antibacterial peptides WP-4 and WP-6, their compositions, and applications, belonging to the fields of antimicrobial peptide technology and biomedicine. This invention obtains a series of antimicrobial peptides by truncating and rationally modifying template peptides to balance the relationship between charge number, hydrophobicity, and amphiphilicity. By measuring antibacterial activity, stability, hemolytic activity, and cytotoxicity, two novel antimicrobial peptides, WP-4 and WP-6, with high activity and low toxicity were obtained, and their amino acid sequences are shown in SEQ ID NO. 5 and SEQ ID NO. 7. The novel antimicrobial peptides obtained by this invention possess broad-spectrum antibacterial activity, good stability under temperature, pH, salt ion, pepsin, and serum conditions, and exhibit no significant hemolytic activity and low cytotoxicity. They are characterized by rapid bactericidal action and low likelihood of inducing drug resistance. Furthermore, the antimicrobial peptides of this invention can enter cells and have a strong inhibitory effect on intracellular bacteria, showing broad application prospects.

The present invention relates to a vancomycin-antimicrobial peptide conjugate and its application. After a cysteine ​​is added to the N-terminus of the antimicrobial peptide M2 ​​for modification, vancomycin and the antimicrobial peptide modified body are coupled through a two-step reaction through a bifunctional protein cross-linking agent sulfo-SMCC. Compared with vancomycin, antimicrobial peptide M2, and a mixture of vancomycin and antimicrobial peptide M2, the vancomycin-antimicrobial peptide conjugate has significantly improved antibacterial activity, overcomes the drug resistance of Gram-positive bacteria to vancomycin, and also produces antibacterial activity against some Gram-negative bacteria, thereby increasing the antibacterial spectrum of vancomycin. At the same time, it also has a stronger anti-biofilm ability, can kill retained bacteria, inhibit bacterial clustering movement, and can also form a synergistic effect with antibiotics to kill bacteria together.

The application discloses an X. laevis modified antibacterial peptide and application thereof, and belongs to the technical field of biological medicine. The X. laevis modified antibacterial peptide is pFG-11K or pFG-11K-8K; the amino acid sequence of pFG-11K is shown as SEQ ID NO. 2; and the amino acid sequence of pFG-11K-8K is shown as SEQ ID NO. 3. The modified antibacterial peptide obtained by modifying the antibacterial peptide pFG of X. laevis has broad-spectrum antibacterial property (especially pFG-11K-8K), has strong bactericidal and bacteriostatic effects on methicillin-resistant Staphylococcus aureus in particular, has almost no hemolytic toxicity on defibrillated horse red blood cells, and can be used for preparing antibacterial drugs.

The invention relates to the technical field of agriculture, animal husbandry and veterinary medicine, in particular to a protease cracking resistant antibacterial peptide FR and application thereof. The invention provides a protease cracking resistant antibacterial peptide FR. The amino acid sequence of the antibacterial peptide FR is as shown in SEQ ID NO. 1. The specific implementation result shows that the protease cracking resistant antibacterial peptide FR provided by the invention has the activity of resisting gram-negative bacteria (escherichia coli, shigella flexneri, salmonella, campylobacter jejuni and the like), also has low hemolytic activity, can resist cracking of high-concentration protease, and has a very good application prospect. In conclusion, the antibacterial peptide FR provided by the invention has the advantages of gastrointestinal tract environment resistance, high salt resistance and protease lysis resistance, can realize the killing effect on gram-negative bacteria in the presence of enzymes and salt ions, has the characteristic of low hemolytic activity, and provides a new way for development of antibiotic substitutes.

The invention discloses a series of honokiol-antibacterial peptide mimic conjugates containing an oxazolethione structure as well as a preparation method and antibacterial application of the honokiol-antibacterial peptide mimic conjugates. The series of compounds take a natural product honokiol as a parent structure, a nitrogen-containing heterocyclic ring is introduced, and then the compound is connected with a hydrophilic small-molecule peptidomimetic fragment, so that a series of honokiol-antibacterial peptide mimic conjugates containing an oxazolethione structure are prepared, and the structural general formula of the honokiol-antibacterial peptide mimic conjugates is shown as a formula (1). The series of compounds have relatively strong in vivo and in vitro antibacterial activity on Staphylococcus aureus ATCC 29213 and clinically isolated methicillin-resistant Staphylococcus aureus (Methicillin-Resistance S. aureus, MRSA), and can be used for preparing the antibacterial agent for treating the staphylococcus aureus, the antibacterial agent for treating the staphylococcus aureus, the antibacterial agent for treating the methicillin-resistant Staphylococcus aureus and the antibacterial agent for treating the methicillin-resistant Staphylococcus aureus, the antibacterial agent for treating the staphylococcus aureus, the antibacterial agent for treating the staphylococcus aureus and the antibacterial agent for treating the staphylococcus aureus. Through structural optimization, the water solubility and antibacterial activity of the compound are enhanced, and the compound has relatively low in-vivo and in-vitro toxicity, hemolytic activity and low drug resistance. Therefore, the honokiol-antibacterial peptide mimic conjugates containing the oxazolethione structure have the potential of being further developed into novel antibacterial drugs. # imgabs0 #

The present invention discloses an antimicrobial peptide AS-12W derived from Chinese alligator, wherein the amino acid sequence of the antimicrobial peptide AS-12W is as shown in SEQ ID NO: 1 or an amino acid sequence having more than 90% homology thereto. The present invention also discloses a preparation method of the antimicrobial peptide and its application. The antimicrobial peptide AS-12W of the present invention has good in vitro and in vivo antibacterial and bactericidal activity against drug-resistant bacteria, and can be used to treat diseases related to drug-resistant bacterial infection. It has the characteristics of a broad antimicrobial spectrum and low hemolytic activity, and can be applied to the fields of medicine, cosmetics, food, etc.

The invention belongs to the technical field of biochemistry, and particularly relates to a derived peptide based on frog-derived antibacterial peptide CPF-C1 as well as a preparation method and application of the derived peptide. The general formula of the derivative peptide is as follows: Trp1-Phe2-X3-X4-Leu5-Leu6-X7-X8-Ala9-Leu10-Arg11-Leu12-Trp13-X14-X15-Val16-Leu17-CONH2, X represents lysine, the lysine at the third site, the lysine at the fourth site, the lysine at the seventh site, the lysine at the eighth site, the lysine at the fourteenth site and the lysine at the fifteenth site can be independently selected from alpha-lysine or epsilon-lysine, and the amino acid at the sixth site to the amino acid at the eleventh site can be independently selected from L-type amino acid or D-type amino acid. The derived peptide obtained by the invention has broad-spectrum antibacterial activity, the antibacterial activity on gram-negative bacteria, especially klebsiella pneumoniae, salmonella typhimurium and pseudomonas aeruginosa is obviously higher than that of a parent peptide CPF-C1, and the derived peptide shows relatively low hemolytic activity and relatively good stability; the compound shows a wide application prospect in preparation of clinical antibacterial drugs.