Total Synthesis of Malacidin A by β-Hydroxyaspartic Acid Ligation-Mediated Cyclization and Absolute Structure Establishment
Research output: Journal Publications and Reviews (RGC: 21, 22, 62) › 21_Publication in refereed journal › peer-review
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Detail(s)
| Original language | English |
|---|---|
| Pages (from-to) | 19868–19872 |
| Journal / Publication | Angewandte Chemie - International Edition |
| Volume | 59 |
| Issue number | 45 |
| Online published | 29 Jul 2020 |
| Publication status | Published - 2 Nov 2020 |
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Abstract
The development of novel antibiotics is critical to combating the growing emergence of drug-resistant pathogens. Malacidin A is a new member of the calcium-dependent antibiotic (CDAs) family with activity against antibiotic-resistant pathogens. Its mode of action is distinct from classical CDAs. However, the absolute structure of malacidin A has not been established. Herein, the total syntheses of malacidin A and its analogues are reported by a combination of Fmoc-based solid-phase peptide synthesis (SPPS) and β-hydroxyaspartic acid ligation-mediated peptide cyclization. The total synthesis enabled us to establish the absolute configuration of malacidin A, which is in agreement with those for natural malacidin A confirmed by advanced Marfey's analysis in our study.
Research Area(s)
- chemical ligation, cyclic peptide antibiotics, malacidin, total synthesis, β-hydroxyaspartic acid
Citation Format(s)
Total Synthesis of Malacidin A by β-Hydroxyaspartic Acid Ligation-Mediated Cyclization and Absolute Structure Establishment. / Sun, Zhenquan; Shang, Zhuo; Forelli, Nicholas et al.
In: Angewandte Chemie - International Edition, Vol. 59, No. 45, 02.11.2020, p. 19868–19872.Research output: Journal Publications and Reviews (RGC: 21, 22, 62) › 21_Publication in refereed journal › peer-review
