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https://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: | Chemical Biology and Drug Design, 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 |
DOI: | 10.1034/j.1399-3011.1999.00095.x |
Published version: | http://dx.doi.org/10.1034/j.1399-3011.1999.00095.x |
Appears in Collections: | Aurora harvest 2 Biochemistry publications |
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