Antibacterial effects of two cecropin type peptides isolated from the silkworm against Salmonella species
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In insect defense system, antimicrobial peptides (AMPs) are one of important biological molecules to survive in a variety of environments. Insect can synthesize AMPs to protect against invading pathogens in humoral immune response. Taking more advantage of biological antimicrobial molecules, we report antibacterial activity of two cecropin type peptides, cecropin and moricin, isolated from the silkworm against four salmonella species. In this work, we purified antimicrobial candidate peptides (AMCP) from the extracts of immune challenged silkworm larval hemolymph by two-step chromatographic purification procedure, cation exchange and gel permeation chromatography. The molecular weights of purified peptides were estimated to be about 4 ~ 5 kDa by Tricin SDS-PAGE analysis, and identified as silkworm cecropin and moricin by NCBI BLAST homology search with their N-terminal amino acid sequences. As antibacterial activity assay, the purified peptides showed stronger antibacterial activity against Salmonella pathogens with an MIC value of 1 ~ 4 μg/mL. Therefore two cecropin type peptides purified from the silkworm will be valuable potential materials for development of new natural antibiotics.
Abstract
In insect defense system, antimicrobial peptides (AMPs) are one of important biological molecules to survive in a variety of environments. Insect can synthesize AMPs to protect against invading pathogens in humoral immune response. Taking more advantage of biological antimicrobial molecules, we report antibacterial activity of two cecropin type peptides, cecropin and moricin, isolated from the silkworm against four salmonella species. In this work, we purified antimicrobial candidate peptides (AMCP) from the extracts of immune challenged silkworm larval hemolymph by two-step chromatographic purification procedure, cation exchange and gel permeation chromatography. The molecular weights of purified peptides were estimated to be about 4 ~ 5 kDa by Tricin SDS-PAGE analysis, and identified as silkworm cecropin and moricin by NCBI BLAST homology search with their N-terminal amino acid sequences. As antibacterial activity assay, the purified peptides showed stronger antibacterial activity against Salmonella pathogens with an MIC value of 1 ~ 4 μg/mL. Therefore two cecropin type peptides purified from the silkworm will be valuable potential materials for development of new natural antibiotics.
참고문헌 (13)
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