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1.C.88 The Chrysophsin (Chrysophsin) Family

Chrysophsin-1 is an amphipathic alpha-helical antimicrobial peptide produced in the gill cells of red sea bream. The peptide has broad range activity against both Gram-positive and Gram-negative bacteria but is more hemolytic than other antimicrobial peptides such as magainin (Mason et al., 2007). Chrysophsin-1 aligns parallel to the membrane surface, and the lipid acyl chains in mixed model membranes are destabilized. The C-terminal RRRH sequence affects the insertion of the peptide into membranes with differing lipid compositions and is crucial for pore formation and toxicity (Mason et al., 2007).

The generalized reaction catalyzed by chrysophsins is:

small molecules (in) small molecules (out)

References associated with 1.C.88 family:

Mason, A.J., P. Bertani, G. Moulay, A. Marquette, B. Perrone, A.F. Drake, A. Kichler, and B. Bechinger. (2007). Membrane interaction of chrysophsin-1, a histidine-rich antimicrobial peptide from red sea bream. Biochemistry. 46: 15175-15187. 18052076