Moricin

Moricin

Solution structure of antibacterial peptide (Moricin) [1]
Identifiers
Symbol Moricin
Pfam PF06451
InterPro IPR009456
SCOP 1kv4
SUPERFAMILY 1kv4
OPM superfamily 160
OPM protein 1kv4

Moricin is a highly basic antibacterial peptide that was isolated from the silkworm Bombyx mori.[2] It consists of a long alpha-helix with 8 turns from a 42 amino acid sequence over almost the entire protein.[2][2] 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.[2][3] Moricin functions as an antibacterial peptide against Gram-positive and Gram-negative bacteria, with its main activity being towards Gram-positive bacteria.[2]

References

  1. Hemmi H, Ishibashi J, Hara S, Yamakawa M (May 2002). "Solution structure of moricin, an antibacterial peptide, isolated from the silkworm Bombyx mori". FEBS Lett. 518 (1-3): 33–8. doi:10.1016/S0014-5793(02)02637-6. PMID 11997013.
  2. 1 2 3 4 5 "ScienceDirect - FEBS Letters : Solution structure of moricin, an antibacterial peptide, isolated from the silkworm Bombyx mori".
  3. Hara S, Ishibashi J, Yamakawa M, Hemmi H (2002). "Solution structure of moricin, an antibacterial peptide, isolated from the silkworm Bombyx mori". FEBS Lett. 518 (1-3): 33–38. doi:10.1016/S0014-5793(02)02637-6. PMID 11997013.

This article incorporates text from the public domain Pfam and InterPro IPR009456

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