Optimized Methods for purification and NMR measurement of antibacterial peptide, bovine lactophoricin
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Lactophoricin (LPcin-I) is a cationic amphipathic peptide with 23-mer peptide, and corresponds to the carboxy terminal 113–135 region of Component-3 of proteose-peptone. LPcin-I is a good candidate as a peptide antibiotic, because it has an antibacterial activity, but no hemolytic activity. On the other hand, its shorter analog (LPcin-II), which corresponds to the 119–135 region of PP3, has no antibacterial activity. In order to understand the structure-activity relationship under the membrane environments, we succeed to produce large amounts of LPcin-I and LPcin-II peptides. Peptides were overexpressed in the form of fusion protein in Escherichia coli, and purified with several chromatography techniques. In this paper, we introduce the optimizing processes of purification and NMR measurement.
Abstract
Lactophoricin (LPcin-I) is a cationic amphipathic peptide with 23-mer peptide, and corresponds to the carboxy terminal 113–135 region of Component-3 of proteose-peptone. LPcin-I is a good candidate as a peptide antibiotic, because it has an antibacterial activity, but no hemolytic activity. On the other hand, its shorter analog (LPcin-II), which corresponds to the 119–135 region of PP3, has no antibacterial activity. In order to understand the structure-activity relationship under the membrane environments, we succeed to produce large amounts of LPcin-I and LPcin-II peptides. Peptides were overexpressed in the form of fusion protein in Escherichia coli, and purified with several chromatography techniques. In this paper, we introduce the optimizing processes of purification and NMR measurement.
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