| Biologically active peptides are currently being investigated for future clinical use as antibiotics and enzyme inhibitors. This investigation focuses on two such peptides from annelids.;Purification of the antimicrobial peptide from the common earthworm ( Lumbricus terrestris) was attempted. Earthworms were extracted with acid, followed by chromatographic techniques. Initially purified by CM cellulose, then followed by Sephadex size separation, and finally HPLC using a C 4 reverse-phase column. The antimicrobial peptide was found to be cationic and 5kDa. Further purification is needed in order to deduce the primary structure.;The primary structure of the CYY50 peptide, from the salivary glands of the Chinese leech (Haemadipsa yanuanesis), was used to predict secondary and tertiary structures. CYY50, a protease inhibitor, was found to be cysteine-rich and exhibits homology to antistasin, hirustasin, and bdellastasin. The predicted tertiary structure will assist in understanding the possible mechanism and future clinical applications. Crystallization is needed to verify results. |
