Solution structure, antibacterial activity, and expression profile of Manduco sexto moricin

In response to wounding or infection, insects produce a battery of antimicrobial peptides (AMPs) and other defense molecules to kill the invading pathogens. To study their structures, functions, and transcriptional regulation, we synthesized Manduca sexta moricin, a 42-residue peptide (GKIPVKAIKQAGKVIGKGLRAINIAGT-rHDVVSFFRPKKKKH, 4539 Da). The compound exhibited potent antimicrobial activities against a broad spectrum of Gram-positive and Gram-negative bacteria with a minimum inhibitory concentration of 1.4 mu m. The mRNA levels of M. sexta moricin increased substantially in fat body and hemocytes after the larvae were challenged with bacterial cells. We determined the solution structure of this AMP by two-dimensional H-1-H-1-nuclear magnetic resonance spectroscopy. The tertiary structure is composed of an eight-turn a-helix spanning almost the entire peptide. Insights of relationships between the structure and function are also presented. Copyright (C) 2008 European Peptide Society and John Wiley & Sons, Ltd.