Primary and secondary structures of grammistins, peptide toxins isolated from the skin secretion of the soapfish Pogonoperca punctata

Autor:	Masami Ishida, Kazuo Shiomi, Hiroshi Yokota, Yuji Nagashima
Rok vydání:	2001
Předmět:	chemistry.chemical_classification Circular dichroism Tertiary amine biology Protein primary structure Peptide Aquatic Science biology.organism_classification Melittin chemistry.chemical_compound chemistry Biochemistry Grammistes sexlineatus Helical wheel Protein secondary structure
Zdroj:	Fisheries Science. 67:163-169
ISSN:	1444-2906 0919-9268
DOI:	10.1046/j.1444-2906.2001.00213.x
Popis:	SUMMARY: Six peptides (grammistins Pp 1, 2a, 2b, 3, 4a and 4b) with both hemolytic and ichthyotoxic activities were isolated from the skin secretion of the soapfish Pogonoperca punctata by gel filtration and reverse-phase high performance liquid chromatography. They were completely sequenced and found to be simple peptides differing from the previous suggestion that they are peculiar peptides with tertiary amine or quaternary ammonium base moieties. Grammistins Pp 1, 2a and 2b were composed of 13 residues, Pp 3 of 25 residues and Pp 4a and 4b of 24 residues. While grammistins Pp 4a and 4b were identical and highly homologous with grammistin Gs 2 previously isolated from another soapfish Grammistes sexlineatus, the other grammistins did not have homologies with any proteinic or peptidic toxins known to date. Judging from circular dichroism data, helical wheel projections and hydrophobic moment plots, all the isolated grammistins are surface-seeking peptides with an abundance in amphiphilic α-helicity, similar to pardaxins from the skin secretion of two species of soles and melittin from bee venom as well as the G. sexlineatus grammistins.
Databáze:	OpenAIRE
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