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The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis . Part 2. Sequence determination using electrospray mass spectrometry 1
Author(s) -
Rozek Tomas,
Bowie John H.,
Wallace John C.,
Tyler Michael J.
Publication year - 2000
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/1097-0231(20001115)14:21<2002::aid-rcm128>3.0.co;2-3
Subject(s) - chemistry , peptide , edman degradation , antibacterial peptide , electrospray , sequence (biology) , mass spectrometry , cyclic peptide , antimicrobial peptides , peptide sequence , biochemistry , antibacterial activity , stereochemistry , bacteria , chromatography , biology , genetics , gene
Sixteen aurein peptides are present in the host defence secretion from the granular dorsal glands of the Green and Golden Bell Frog Litoria aureus and seventeen from those of the related Southern Bell Frog Litoria raniformis . All peptides have been sequenced using a combination of electrospray mass spectrometry and Lys‐C digestion, with each sequence confirmed by automated Edman sequencing. The peptides are named in five groups, viz. aureins 1–5. Ten of these peptides are common to both species of frog. Thirteen of the aurein peptides show wide‐spectrum antibiotic and anticancer activity. Amongst the more active peptides are aurein 1.2 (GLFDIIKKIAESF‐NH 2 ), the smallest peptide from an anuran reported to have both antibiotic and anticancer activity; aurein 2.2 (GLLDIVKKVIGAFGSL‐NH 2 ) and aurein 3.1 (GLFDIVKKIAGHIAGSI‐NH 2 ). The aurein 4 and 5 peptides, e.g. aurein 4.1 (GLIQTIKEKLKELAGGLVTGIQS‐OH) and aurein 5.1 (GLLDIVTGLLGNLIVDVLKPKTPAS‐OH), show neither antibacterial nor anticancer activity. Copyright © 2000 John Wiley & Sons, Ltd.