The solution structure of uperin 3.6, an antibiotic peptide from the granular dorsal glands of the Australian toadlet, Uperoleia mjobergii.
Uperin 3.6 (GVIDA5AKKVV10NVLKN15LF-NH2) is a wide-spectrum antibiotic peptide isolated from the Australian toadlet, Uperoleia mjobergii. With only 17 amino acid residues, it is smaller than most other wide-spectrum antibiotic peptides isolated from amphibians. In 50% (by vol.) trifluoroethanol, an NMR study and structure calculations indicate that uperin 3.6 adopts a well-defined amphipathic alpha-helix with distinct hydrophilic and hydrophobic faces. Examination of the activities of synthetic modifications of uperin 3.6 reveal that the three lysine residues are essential for antibiotic activity.
Chia
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Department of Chemistry, The University of Adelaide, South Australia, Australia.
Carver
J A
JA
Mulhern
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Bowie
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JH
D000595:Amino Acid Sequence; D029845:Amphibian Proteins; D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry*; D001001:Anura; D002942:Circular Dichroism; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010455:Peptides; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012867:Skin / Q000737:chemistry*
D029845:Amphibian Proteins; D000900:Anti-Bacterial Agents; D010455:Peptides; D011506:Proteins; C121472:uperin 3.6 peptide, Uperoleia mjobergii