Antimicrobial Peptide Synthesis (AMPs)
Antimicrobial peptides (AMPs) are cationic peptides in most organisms, which constitute an important part of the biological immune system. Antimicrobial peptides have broad-spectrum and high-efficiency antimicrobial activity and cell selectivity. Their unique membrane destruction mechanism is not easy to cause drug resistance mutation of pathogens, which is expected to become an effective "antibiotic" for controlling pathogens.
At present, there are more than 3000 kinds of antimicrobial peptides from different organisms. Based on the antimicrobial peptide database in 2016, the distribution of antimicrobial peptide sources is analyzed：Animals (76%), plants (13%) and bacteria (1.8%) are the main sources of natural antimicrobial peptides.In the early stage, all natural antimicrobial peptides were extracted and separated directly from organisms by researchers, but this method is relatively difficult, low yield, high technical requirements and high cost, which can not be used in large-scale peptides production of antimicrobial .
Omizzur mainly use solid phase method to synthesize antimicrobial peptides, which is mainly through the connection of chemical groups on the solid resin carrier with the carboxyl end of amino acids, then the protective group of amino acids (protected amino acids) is removed, the next amino acid is connected.By repeating the above steps, the peptide with clear sequence is obtained. Finally, the peptide is removed from the resin with corresponding chemical reagent.Most AMPs consist of 12-80 amino acids,which have been proved to eliminate bacteria, yeasts, fungi, viruses and in some cancerous cells.
• Rich experience in peptide synthesis
Omizzur have more than 10 years of experience in the synthesis of active peptides,accumulated a lot of synthesis knowledge and skills for antimicrobial peptides which derived from animal ,plant and bacterial .
• Synthesis of secondary structure for AMPs
Omizzur has ability to synthesize complex antibacterial peptides with α - helix structure, β - fold structure, combination for α - helix structure and β - fold structure.
OMIZZUR’s synthesis of antimicrobial peptides
|Gomesin||QCRRLCYKQRCVTYCRGR||Spider Acanthoscurria gomesiana|
|Magainin-St1||GLKEVAHSAKKFAKGFISGLTGS||African clawed frog|
√ Antimicrobial peptides and its polymers are promising substitutes for antibiotics, which are expected to solve the problem of drug resistance caused by regular antibiotics.
√ Antimicrobial peptides can destroy mitochondria and cause programmed cell death. By optimizing the structure of antibacterial peptide can enhance the anti-cancer effect and be widely used in anti-cancer research
√ Clinical trials for local treatment: skin tissue, lung and intestinal infections.It can improve immunity and accelerate wound healing also.
√ Genetic engineering research for plant disease resistance.Antimicrobial peptides have fungicidal activity against a variety of plant pathogens, and the expression of antimicrobial peptide gene in the plant can improve its disease resistance.
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3. Dathe M, Wieprecht T.Structural features of helical antimicrobia peptides：their potential to modulate activity on model membrances and biological cells.Biochim Biophys Acta,1999,1465:71-87
4. SCOTT MG, YAN H , HANCOCK RW . Biological properties of structurally related a-Helical cationic antimicrobial peptides,INFECT IMMUN,1999,67:2005-2009.
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