Heteroatom‐interchanged isomers of lissoclinamide 5: Copper(II) complexation, halide binding, and biological activity
Cyclic peptides found in nature are often proposed as biological metal chelators owing to their cavitand architectures. This theory was probed by synthesizing and evaluating the physical and biological properties of heteroatom‐interchanged variants. A comprehensive study reaffirmed that small struct...
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| Main Authors: | , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
25 March 2018
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| In: |
European journal of organic chemistry
Year: 2018, Issue: 12, Pages: 1465-1476 |
| ISSN: | 1099-0690 |
| DOI: | 10.1002/ejoc.201701659 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1002/ejoc.201701659
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| Author Notes: | Sida Xie, Andrei I. Savchenko, Marion Kerscher, Rebecca L. Grange, Elizabeth H. Krenske, Jeffrey R. Harmer, Michelle J. Bauer, Natasa Broit, Dianne J. Watters, Glen M. Boyle, Paul V. Bernhardt, Peter G. Parsons, Peter Comba, Lawrence R. Gahan, and Craig M. Williams |
| Summary: | Cyclic peptides found in nature are often proposed as biological metal chelators owing to their cavitand architectures. This theory was probed by synthesizing and evaluating the physical and biological properties of heteroatom‐interchanged variants. A comprehensive study reaffirmed that small structural changes induce dramatic effects in complexation, halide binding, and biological activity. |
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| Item Description: | Gesehen am 16.04.2020 |
| Physical Description: | Online Resource |
| ISSN: | 1099-0690 |
| DOI: | 10.1002/ejoc.201701659 |