Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/11338
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Type: Journal article
Title: The solution structure of uperin 3.6, an antibiotic peptide from the granular dorsal glands of the Australian toadlet, Uperoleia mjobergii
Author: Chia, B.
Carver, J.
Mulhern, T.
Bowie, J.
Citation: Journal of Peptide Research, 1999; 54(2):137-145
Publisher: MUNKSGAARD INT PUBL LTD
Issue Date: 1999
ISSN: 1397-002X
1399-3011
Statement of
Responsibility: 
B.C.S. Chia, J.H. Bowie, J.A. Carver and T.D. Mulhern
Abstract: 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 α-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.
Keywords: Antibiotic peptides; NMR spectroscopy; solution structure; toadlet; uperin 3.6; Uperoleia mjobergii
Rights: © Munksgaard International Publishers Ltd, 1999
RMID: 0030004377
DOI: 10.1034/j.1399-3011.1999.00095.x
Appears in Collections:Biochemistry publications

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