Antimicrobial peptide

Antibiotic administration is the current method of choice to fight a bacterial infection. However, due to over-use of antibiotics, drug-resistant bacteria have emerged and frequently appear. This complication makes decreases wound healing potential and makes recovery increasingly difficult. Currently, more focus has been placed on new anti-infectious agents to fight these drug-resistant pathogens. Antimicrobial peptides (AMPs) are stable peptides that have extensive abilities to kill or inhibit the growth of bacteria. They play a role in defense mechanism for all organisms, ranging from prokaryotes to humans. Some peptides act against specific strains of microbes. Unlike antibiotics, AMPs use their chargeability to interact with bacteria cell membrane. Than use hydrophobic region interfere the membrane structure. This leads to cell lysis and bypasses bacterial antibiotic drug-resistance mechanisms. [1] AMPs also functions in multiple roles in the immune system. Through target specificity, charge and bacterial toxicity, AMPs have the ability to alter the properties of mammalian cells and help in wound healing.[2] We choose two types of AMPs, Signiferin and Epinecidin-1, as our reagents. Signiferin is a peptide derived from the skin mucus of Crinia signifera (tree frog). It has demonstrated effectiveness in killing MRSA, and has been proven by the TU-Delft 2013 iGEM team.[3] Epinecidin-1 is a peptide originating from the skin mucus of Epinephelus coioides. It has ability to help wound healing and has been proven by animal studies.[4]

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