Moricin is a highly basic antibacterial peptide that was isolated from the silkworm Bombyx mori.[1] It consists of a long alpha-helix with 8 turns from a 42 amino acid sequence over almost the entire protein.[1] The amphipathic N-terminal segment of the alpha- helix is mainly responsible for the increase in permeability of the bacterial membrane which kills the bacteria.[1] Moricin functions as an antibacterial peptide against Gram-positive and Gram-negative bacteria, with its main activity being towards Gram-positive bacteria.[1]

References

  1. ^ a b c d e Hemmi H, Ishibashi J, Hara S, Yamakawa M (May 2002). "Solution structure of moricin, an antibacterial peptide, isolated from the silkworm Bombyx mori". FEBS Letters. 518 (1–3): 33–8. doi:10.1016/S0014-5793(02)02637-6. PMID 11997013. S2CID 23886673.
This article incorporates text from the public domain Pfam and InterPro: IPR009456
Allikas: https://en.wikipedia.org/wiki/Moricin
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