Description
Cecropins (cecropins) is the first animal antibacterial peptide to be discovered. It was isolated from the chrysalis pupae in 1980. This type of peptide antibiotic generally contains 37 to 39 amino acid residues, does not contain cysteine, and its N-terminal region is strongly alkaline, which can form a nearly perfect parent helical structure. A hydrophobic helix can be formed in the C-terminal region, and there is a hinge region formed by glycine and proline between the two. The C-terminal of most peptides is amidated, and amidation plays an important role in its antibacterial activity.
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