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Concise Chemoenzymatic Total Synthesis and Identification of Cellular Targets of Cepafungin I.
Amatuni A, Shuster A, Adibekian A, Renata H. Amatuni A, et al. Cell Chem Biol. 2020 Oct 15;27(10):1318-1326.e18. doi: 10.1016/j.chembiol.2020.07.012. Epub 2020 Aug 6. Cell Chem Biol. 2020. PMID: 32763140 Free PMC article.
The natural product cepafungin I was recently reported to be one of the most potent covalent inhibitors of the 20S proteasome core particle through a series of in vitro activity assays. ...This study lays the groundwork for further medicinal chemistry exploration to …
The natural product cepafungin I was recently reported to be one of the most potent covalent inhibitors of the 20S proteasome …
Comprehensive Structure-Activity Relationship Studies of Cepafungin Enabled by Biocatalytic C-H Oxidations.
Amatuni A, Shuster A, Abegg D, Adibekian A, Renata H. Amatuni A, et al. ACS Cent Sci. 2023 Jan 27;9(2):239-251. doi: 10.1021/acscentsci.2c01219. eCollection 2023 Feb 22. ACS Cent Sci. 2023. PMID: 36844499 Free PMC article.
This Article chronicles the development of a chemoenzymatic approach to cepafungin I. A failed initial route involving derivatization of pipecolic acid prompted us to examine the biosynthetic pathway for the production of 4-hydroxylysine, which culminated in the dev …
This Article chronicles the development of a chemoenzymatic approach to cepafungin I. A failed initial route involving derivat …
Activation, Structure, Biosynthesis and Bioactivity of Glidobactin-like Proteasome Inhibitors from Photorhabdus laumondii.
Zhao L, Le Chapelain C, Brachmann AO, Kaiser M, Groll M, Bode HB. Zhao L, et al. Chembiochem. 2021 May 4;22(9):1582-1588. doi: 10.1002/cbic.202100014. Epub 2021 Mar 3. Chembiochem. 2021. PMID: 33452852 Free PMC article.
The glidobactin-like natural products (GLNPs) glidobactin A and cepafungin I have been reported to be potent proteasome inhibitors and are regarded as promising candidates for anticancer drug development. ...
The glidobactin-like natural products (GLNPs) glidobactin A and cepafungin I have been reported to be potent proteasome inhibi …
Optical Control of Proteasomal Protein Degradation with a Photoswitchable Lipopeptide.
Morstein J, Amatuni A, Shuster A, Kuttenlochner W, Ko T, Abegg D, Groll M, Adibekian A, Renata H, Trauner DH. Morstein J, et al. Angew Chem Int Ed Engl. 2024 Feb 19;63(8):e202314791. doi: 10.1002/anie.202314791. Epub 2024 Jan 16. Angew Chem Int Ed Engl. 2024. PMID: 38109686
Herein, we present the application of photoswitching to a lipidated natural product, the potent proteasome inhibitor cepafungin I. Several azobenzene-containing lipids were attached to the cyclopeptide core, yielding photoswitchable derivatives. ...In a proteome-wid …
Herein, we present the application of photoswitching to a lipidated natural product, the potent proteasome inhibitor cepafungin I …
Evaluation of the Antifungal Activities of Photorhabdus akhurstii and Its Secondary Metabolites against Phytopathogenic Colletotrichum gloeosporioides.
Tu PW, Chiu JS, Lin C, Chien CC, Hsieh FC, Shih MC, Yang YL. Tu PW, et al. J Fungi (Basel). 2022 Apr 15;8(4):403. doi: 10.3390/jof8040403. J Fungi (Basel). 2022. PMID: 35448634 Free PMC article.
We identified the bioactive ingredients of P. akhurstii sp. nov. 0813-124 to be glidobactin A and cepafungin I, with MIC values lower than 1.5 and 2.0 g/mL, respectively. ...
We identified the bioactive ingredients of P. akhurstii sp. nov. 0813-124 to be glidobactin A and cepafungin I, with MIC value …
One-shot NMR analysis of microbial secretions identifies highly potent proteasome inhibitor.
Stein ML, Beck P, Kaiser M, Dudler R, Becker CF, Groll M. Stein ML, et al. Proc Natl Acad Sci U S A. 2012 Nov 6;109(45):18367-71. doi: 10.1073/pnas.1211423109. Epub 2012 Oct 22. Proc Natl Acad Sci U S A. 2012. PMID: 23091006 Free PMC article.
The technique was applied for analysis of the different life stages of the bacterium Photorhabdus luminescens, which resulted in the isolation and characterization of cepafungin I (CepI), the strongest proteasome inhibitor described to date. ...
The technique was applied for analysis of the different life stages of the bacterium Photorhabdus luminescens, which resulted in the isolati …
Structures of cepafungins I, II and III.
Terui Y, Nishikawa J, Hinoo H, Kato T, Shoji J. Terui Y, et al. J Antibiot (Tokyo). 1990 Jul;43(7):788-95. doi: 10.7164/antibiotics.43.788. J Antibiot (Tokyo). 1990. PMID: 2387773 Free article.
Isolation of cepafungins I, II and III from Pseudomonas species.
Shoji J, Hinoo H, Kato T, Hattori T, Hirooka K, Tawara K, Shiratori O, Terui Y. Shoji J, et al. J Antibiot (Tokyo). 1990 Jul;43(7):783-7. doi: 10.7164/antibiotics.43.783. J Antibiot (Tokyo). 1990. PMID: 2387772 Free article.