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([a]D23 = À51.2, c = 0.8, pH 7 phosphate buffer) was consis-
Acknowledgements
tent with that of the natural product ([a]D20 = À48, c = 1, pH 7
phosphate buffer), which unambiguously establishes the
absolute configurations of AMA. Moreover, we applied the
same synthetic route to obtain the other two possible isomers
(R,S,S)-AMA and (S,R,S)-AMA. The 1H and 13C NMR
spectra of these two isomers did not fully match those of
the natural isolate.[19] Collectively, the results unambiguously
show that the configuration of AMA should be reassigned as
(S,S,S).
We thank Prof. Gerard Wright (McMaster University) for
generously providing us the authentic natural product sample
for spectra comparison. We also thank Dr. Alexander Jones,
Dr. Chao Li, and Dr. Houhua Li for helpful discussions, as
well as Prof. Changwen Jin and Prof. Hongwei Li (Peking
University) for the assistance with 600 MHz NMR analysis.
Financial support from the National High Technology Project
973 (2015CB856200) and NNSFC (21222209, 91313303, and
21472010) is gratefully acknowledged.
Wright and co-workers have demonstrated that the
natural product AMA has good in vitro dose-dependent
inhibition against metallo-b-lactamase NDM-1 and related
MBLs such as VIM-2.[11a] To validate the NDM-1 inhibition
activity of our synthetic samples, we performed an enzyme
inhibition assay with the purified NDM-1 protein and nitro-
cefin as a substrate (Figure 2).[19] As expected, the revised
Keywords: antibiotics · aspergillomarasmine A ·
metallo-b-lactamase · structural reassignment · total synthesis
How to cite: Angew. Chem. Int. Ed. 2016, 55, 4291–4295
Angew. Chem. 2016, 128, 4363–4367
[3] For a recent review, see: M. S. Masoud, A. E. Ali, N. M. Nasr, J.
Chem. Pharm. Res. 2014, 6, 28 – 58.
[7] D. Yong, M. A. Toleman, C. G. Giske, H. S. Cho, K. Sundman, K.
Figure 2. Inhibition of NDM-1 by (S,S,S)-AMA. (S,S,S)-AMA (white
circles) inhibits NDM-1 with a half-maximal inhibitory concentration
(IC50) value of 8.1 mm, while (R,R,S)-AMA shows no inhibition activity
against NDM-1.
[9] G. Patel, R. A. Bonomo, Front. Microbiol. 2013, 4, 48.
[10] For excellent reviews on antibacterial natural products, see: a) F.
von Nussbaum, M. Brands, B. Hinzen, S. Weigand, D. Haebich,
the discovery of new antibiotics from natural product isolation,
see: c) L. L. Ling, T. Schneider, A. J. Peoples, A. L. Spoering, I.
Engels, B. P. Conlon, A. Mueller, T. F. Schaberle, D. E. Hughes,
S. Epstein, M. Jones, L. Lazarides, V. A. Steadman, D. R. Cohen,
C. R. Felix, K. A. Fetterman, W. P. Millett, A. G. Nitti, A. M.
Gavrish, C. S. Sit, S. Cao, O. Kandror, A. Spoering, A. Peoples,
L. Ling, A. Fetterman, D. Hughes, A. Bissell, H. Torrey, T.
Akopian, A. Mueller, S. Epstein, A. Goldberg, J. Clardy, K.
on chemical synthesis in antibiotic discovery, see: e) P. M.
examples of the development of new antibiotics based on natural
product synthesis, see: f) A. Okano, A. Nakayama, K. Wu, E. A.
Lindsey, A. W. Schammel, Y. Feng, K. C. Collins, D. L. Boger, J.
Wright, C. D. Lerner, K. Noson, M. Charest, D. R. Siegel, Y.-M.
i) M. G. Charest, C. D. Lerner, J. D. Brubaker, D. R. Siegel,
structure (S,S,S)-AMA (2) showed significant in vitro dose-
dependent inhibition of NDM-1. Interestingly, the originally
proposed structure (R,R,S)-AMA (1) showed no inhibition of
NDM-1 whatsoever. Thus, both our biological and chemical
studies confirm that natural AMA should have the reassigned
structure 2. Furthermore, this interesting result provides
initial leads for the development of more effective AMA-
derived antibiotics.
In summary, we have accomplished the first total synthesis
of the natural product aspergillomarasmine A, a potent and
selective inhibitor of NDM-1. In the course of our synthetic
studies, we reassigned the stereochemical configurations of
the originally proposed structure of AMA. The structurally
revised synthetic AMA was confirmed to have same inhib-
itory effect on NDM-1 as the naturally occurring AMA. We
have also developed an effective late-stage oxidation strategy
and a robust global deprotection method that might find
further synthetic application in peptide natural product
synthesis. Notably, our synthesis features a convergent, flex-
ible, and stereocontrolled route that is amenable to the
efficient preparation of analogues. Studies towards the
development of more potent and selective metallo-b-lacta-
mase inhibitors based on AMA are currently ongoing in our
laboratory.
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Angew. Chem. Int. Ed. 2016, 55, 4291 –4295