Peptides and their uses

An integer, free technology, applied in the field of molecular biology and biochemistry, can solve the problems of the increase of antibiotic-resistant bacteria and the overuse of antibiotics

Inactive Publication Date: 2015-08-12
AGENCY FOR SCI TECH & RES +1
View PDF1 Cites 9 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, due to the overuse of antibiotics in all aspects of life, antibiotic resistant bacteria are increasing

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Peptides and their uses
  • Peptides and their uses
  • Peptides and their uses

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 3

[0171] Example 3 Time-kill kinetics

[0172] Materials and Methods

[0173] The bacteria used in the time-kill study were isolated from 18-20 hour Tryptic Soy Agar (TSA) plates. Then, the inoculum was suspended in 0.31 mM phosphate buffer and adjusted to obtain 10 5 To 10 6 CFU / mL bacterial suspension. Then, the inoculum was treated with various concentrations of C8V2D. The mixture was incubated at 35°C. Remove aliquots of the culture at 0 minutes, 10 minutes, 30 minutes, 1 hour, 2 hours, 5 hours, and 24 hours for the plate viable count. Use Dey-Engley Neutralization Broth (Dey-Engley Neutralization Broth) 10-fold serial dilution aliquots, and then use the surface coating plate method to spread 20 μL of each dilution onto TSA flat. Then, the plate was incubated at 35°C for 48 hours to 72 hours. Cell viability was evaluated by counting the colonies grown on the plate. Bactericidal activity was defined as a 3 log reduction in viable counts (3-log) in cultures treated with anti...

Embodiment 4

[0175] Example 4 In vitro and in vivo toxicity

[0176] 4A. Determination of hemolysis

[0177] Materials and Method

[0178] Fresh red blood cells (RBC) from New Zealand white rabbits were used in this experiment. The obtained RBC was centrifuged at 3000 rpm for 10 minutes. The supernatant was removed and washed twice with sterile PBS buffer (20mM, 100mM NaCl, pH 7). The RBC was further diluted to 8% stock solution in PBS. The peptide is dissolved in PBS at the desired storage concentration. When the compound was mixed with RBC, the desired concentration of 4% RBC was obtained. For C14V2D and C16V2D, dissolve them in dimethylformamide ((CH 3 ) 2 NCH; DMF). When the compound was mixed with RBC, the desired concentration of 4% RBC and 0.5% DMF was obtained. A DMF concentration of less than 1% was used because it has negligible hemolytic activity on RBC. The mixture was added to a 1.5 mL centrifuge tube and incubated at 37°C for 1 hour. After incubation, the blood was centrifu...

Embodiment 5

[0206] Example 5 Lipopolysaccharide (LPS) neutralization study

[0207] Study the possible effects of peptides and lipid-modified peptides of the present disclosure on LPS of Gram-negative bacteria

[0208] Materials and Method

[0209] The lipopolysaccharide (LPS) neutralization was evaluated by using the Pierce Limulus Amebocyte Lysate (LAL) Chromogenic Endotoxin Quantitative Kit (Thermo Scientific) with minor modifications to the manufacturer's protocol. LAL contains enzymes that are activated in a series of reactions in the presence of LPS. The last enzyme activated in the cascade splits the chromophore from the chromonic substrate into p-nitroaniline (PNA) and produces a yellow color. The amount of PNA released will be measured photometrically at 405 nm, which is proportional to the amount of LPS in the system. In short, first equilibrate the microplate in a heating module at 37°C for 10 minutes. Then, the lipid-modified peptide of the desired concentration was pipetted into...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

PUM

No PUM Login to view more

Abstract

Disclosed are antimicrobial peptides. Also disclosed are methods of treating bacterial infection and fungal infection and a method of removing biofilm. Also disclosed is the use of these peptides.

Description

[0001] Cross reference of related applications [0002] This application claims the right of priority to Singapore Patent Application No. 201206671-8 filed on September 7, 2012, the content of which is hereby incorporated by reference in its entirety for all purposes. Invention field [0003] The present invention generally relates to the fields of molecular biology and biochemistry and particularly relates to antimicrobial peptides and their methods of use and uses. Background of the invention [0004] Antimicrobial agents are agents used to inhibit the growth of microorganisms or kill microorganisms. Various antimicrobial agents such as antibiotics or antibacterial agents, antifungal agents, antiviral agents or antiparasitic agents are known in the art. The most commonly known antimicrobial agents are antibiotics, which can be applied to a variety of applications in the medical or non-medical sectors. However, due to the abuse of antibiotics in all aspects of life, antibiotic-re...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

Application Information

Patent Timeline
no application Login to view more
Patent Type & Authority Applications(China)
IPC IPC(8): C07K14/00C07K7/00A61K38/04A61K38/10A61K38/16A61P31/04A61P31/10A61L12/14
CPCC07K7/08A61K38/00C07K14/00A61K38/04A61K38/10A61K38/16C07K7/00A61P1/12A61P27/02A61P31/04A61P31/10A61P39/02Y02A50/30A61K45/06
Inventor 韦尔马·钱德拉谢卡尔李建国拉克斯米尼亚拉扬·拉詹玛尼罗杰·威尔默·博伊尔曼刘守平许俊杰
Owner AGENCY FOR SCI TECH & RES
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Try Eureka
PatSnap group products