Various kinds of biologically active peptides have previously been isolated from the skin secretions of Amolops loloensis frog,such as antimicrobial peptides,bradykinin-like peptides and algesic peptides.A novel insul...Various kinds of biologically active peptides have previously been isolated from the skin secretions of Amolops loloensis frog,such as antimicrobial peptides,bradykinin-like peptides and algesic peptides.A novel insulinotropic peptide named amolopin was identified in A.loloensis frog’s skin secretion.Its primary structure sequence was determined by Edman degradation as:FLPIVGKSLSGLSGKL-NH2.BLAST search indicates that the amino acid sequence of amolopin is quite different from other known insulin secretagogues,including mastoparan,exendins and a-latrotoxin,nor does it like incretins(e.g.glucagons like peptide-1 and glucose-dependent insulinotropic ploypeptide)either.However,amolopin shows certain structural similarity with amphibian antimicrobial temporins and vespid chemotactic peptides isolated from Vespa magnifica.Amolopin can stimulate insulin release in INS-1 cells in a dose-dependent manner.Primary investigation on its action mechanisms reveals that amolopin does not increase the influx of Ca2?.In conclusion,a novel 16-amino acid peptide with insulin-releasing activity is initially discovered from the skin secretion of A.loloensis frog.Further work is necessary to evaluate its potential as novel anti-diabetic candidate.展开更多
文摘Various kinds of biologically active peptides have previously been isolated from the skin secretions of Amolops loloensis frog,such as antimicrobial peptides,bradykinin-like peptides and algesic peptides.A novel insulinotropic peptide named amolopin was identified in A.loloensis frog’s skin secretion.Its primary structure sequence was determined by Edman degradation as:FLPIVGKSLSGLSGKL-NH2.BLAST search indicates that the amino acid sequence of amolopin is quite different from other known insulin secretagogues,including mastoparan,exendins and a-latrotoxin,nor does it like incretins(e.g.glucagons like peptide-1 and glucose-dependent insulinotropic ploypeptide)either.However,amolopin shows certain structural similarity with amphibian antimicrobial temporins and vespid chemotactic peptides isolated from Vespa magnifica.Amolopin can stimulate insulin release in INS-1 cells in a dose-dependent manner.Primary investigation on its action mechanisms reveals that amolopin does not increase the influx of Ca2?.In conclusion,a novel 16-amino acid peptide with insulin-releasing activity is initially discovered from the skin secretion of A.loloensis frog.Further work is necessary to evaluate its potential as novel anti-diabetic candidate.