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1.C.81 The Arenicin (Arenicin) Family

The solution structure and the mode of action of arenicin isoform 1, an antimicrobial peptide with a unique 18-residue loop structure, from the lugworm Arenicola marina have been elucidated (Andra et al., 2007). Arenicin folds into a two-stranded anti-parallel β-sheet. It exhibits high antibacterial activity against Gram-negative and positive bacteria, as well as yeast. Bacterial killing occurs within minutes and is accompanied by membrane permeabilisation, membrane detachment, and release of cytoplasmic constituents (Andra et al., 2007).

Arenicin is a hydrophilic protein, 202 aas long with a single N-terminal hydrophobic region. The last 21 residues (182-202 aas) form the processed active peptide. The protein also contains a BRICHOS domain (pfam 64089) found in proteins involved in dementia and cancer. The full length protein is homologous to the chondromodulin-1 precursor (P17404) also called 'leukocyte cell-derived chemotaxin-1' of H. sapiens.

References associated with 1.C.81 family:

Andrä, J., I. Jakovkin, J. Grötzinger, O. Hecht, A.D. Krasnosdembskaya, T. Goldmann, T. Gutsmann, and M. Leippe. (2008). Structure and mode of action of the antimicrobial peptide arenicin. Biochem. J. 410(1): 113-122. 17935487
Shenkarev, Z.O., S.V. Balandin, K.I. Trunov, A.S. Paramonov, S.V. Sukhanov, L.I. Barsukov, A.S. Arseniev, and T.V. Ovchinnikova. (2011). Molecular mechanism of action of β-hairpin antimicrobial peptide arenicin: oligomeric structure in dodecylphosphocholine micelles and pore formation in planar lipid bilayers. Biochemistry 50: 6255-6265. 21627330