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CAT# | Product Name | M.W | Molecular Formula | Inquiry |
---|---|---|---|---|
A10002 | Alloferon 2 | 1128.2 | Inquiry | |
A35001 | Apidaecin | Inquiry | ||
A35002 | Apidaecin-1B | Inquiry | ||
A35003 | Apidaecin-1A | Inquiry | ||
A35004 | Apidaecin-2 | Inquiry | ||
A35006 | Apidaecin Ho+ | Inquiry | ||
A35007 | Usp45 protein | Inquiry | ||
C13002 | Cecropin A (1-7)-Melittin A (2-9) amide | 1770.33 | C89H152N22O15 | Inquiry |
C13003 | Cecropin A (1-8)-Melittin (1-18) amide | 2794.55 | C136H233N33O29 | Inquiry |
C13005 | Cecropin P1 (porcine) | 3338.90 | C147H253N45O43 | Inquiry |
C13006 | Cecropin B, Free Acid | 3835.7 | C176H301N51O42S1 | Inquiry |
In the 1980s, antimicrobial peptides are discovered by the Swedish scientist Boman. Antimicrobial peptides are encoded by genes in ribosomes. Antimicrobial peptides can be generally classified into four categories according to their different sources, namely antimicrobial peptides derived from insects, animals, and microbial genetically engineered bacteria. To date, more than 1,500 antimicrobial peptides from different sources have been reported. Different types of antimicrobial peptides usually have the following characteristics: short chain, strong cationic, good thermal stability, no drug shielding and does not affect eukaryotic cells. Antibacterial peptides usually act on bacteria and play an important role in the immune response of eukaryotes.
The antimicrobial peptide is capable of interacting with the cell membrane surface to alter the permeability of the membrane. The positively charged region of the cationic antimicrobial peptide interacts with the negatively charged region on the cell membrane to insert the hydrophobic end of the antimicrobial peptide molecule into the lipid membrane of the cell membrane, thereby altering the lipid membrane structure. The antimicrobial peptide forms a transmembrane potential after interacting with the cell membrane, breaking the acid-base balance, affecting the osmotic pressure, and inhibiting the respiration. The interaction between the antimicrobial peptide and the membrane is directly related to the antibacterial activity of the antimicrobial peptide.
Today, antimicrobial peptides from different sources are becoming increasingly significant. Antibacterial peptides have been applied to various fields, such as medicine, food preservation, food additives, etc. What’s more, antimicrobial peptides have received widespread attention from researchers all over the world in the research of anti-tumor. Antimicrobial peptides have high-efficiency, broad-spectrum antibacterial activity, and potential anti-tumor activity. In addition, antimicrobial peptide is also able to accelerate the immune response and wound healing, making it a new drug to replace traditional antibiotics drugs.
References
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