Micropeptin EI-964 is a cyclic peptide compound isolated from a marine cyanobacterium with potent inhibitory activity against serine proteases, particularly chymotrypsin and trypsin. It has shown promising activity ag...Micropeptin EI-964 is a cyclic peptide compound isolated from a marine cyanobacterium with potent inhibitory activity against serine proteases, particularly chymotrypsin and trypsin. It has shown promising activity against various cancer cell lines, making it a candidate for drug development. The unique structure and activity of Micropeptin EI-964 make it a promising lead compound for the development of novel serine protease inhibitors and anti-cancer drugs. Computational Chemistry and Molecular Modeling techniques can provide valuable insights into the chemical reactivity and pharmaceutical properties of Micropeptin EI-964, guiding the design and development of new compounds with enhanced bioactivity and improved drug-like properties.展开更多
The gene cluster for the biosynthetic of a nonribosomal peptide, cyanopeptolins and micropeptin (MCN), was identified in Microcystis strains and halogenated MCN-producing Microcystis were found to possess the halogena...The gene cluster for the biosynthetic of a nonribosomal peptide, cyanopeptolins and micropeptin (MCN), was identified in Microcystis strains and halogenated MCN-producing Microcystis were found to possess the halogenase gene, mcnD, between nonribosomal peptide synthetase genes, mcnC and mcnE. A comparative sequence analysis of the mcn gene cluster between halogenated and non-halogenated MCN-producing strains revealed mosaic sequence traces from mcnD in the non-coding region between mcnC and mcnE in the latter strains. A phylogenetic analysis based on a 170-bp non-coding region including the mcnD traces suggests that the recombination events occurred in a particular region of the Microcystis’ mcn gene. This study provides novel insight into the ecological patterning of widespread Microcystis species.展开更多
文摘Micropeptin EI-964 is a cyclic peptide compound isolated from a marine cyanobacterium with potent inhibitory activity against serine proteases, particularly chymotrypsin and trypsin. It has shown promising activity against various cancer cell lines, making it a candidate for drug development. The unique structure and activity of Micropeptin EI-964 make it a promising lead compound for the development of novel serine protease inhibitors and anti-cancer drugs. Computational Chemistry and Molecular Modeling techniques can provide valuable insights into the chemical reactivity and pharmaceutical properties of Micropeptin EI-964, guiding the design and development of new compounds with enhanced bioactivity and improved drug-like properties.
文摘The gene cluster for the biosynthetic of a nonribosomal peptide, cyanopeptolins and micropeptin (MCN), was identified in Microcystis strains and halogenated MCN-producing Microcystis were found to possess the halogenase gene, mcnD, between nonribosomal peptide synthetase genes, mcnC and mcnE. A comparative sequence analysis of the mcn gene cluster between halogenated and non-halogenated MCN-producing strains revealed mosaic sequence traces from mcnD in the non-coding region between mcnC and mcnE in the latter strains. A phylogenetic analysis based on a 170-bp non-coding region including the mcnD traces suggests that the recombination events occurred in a particular region of the Microcystis’ mcn gene. This study provides novel insight into the ecological patterning of widespread Microcystis species.
