Chemical synthesis of tripeptide thioesters for the biotechnological incorporation into the myxobacterial secondary metabolite argyrin via mutasynthesis.
Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Your vote was cast
Thank you for your feedback
Thank you for your feedback
AuthorsSiebert, David C B
Wenzel, Silke C
MetadataShow full item record
AbstractThe argyrins are secondary metabolites from myxobacteria with antibiotic activity against Pseudomonas aeruginosa. Studying their structure-activity relationship is hampered by the complexity of the chemical total synthesis. Mutasynthesis is a promising approach where simpler and fully synthetic intermediates of the natural product's biosynthesis can be biotechnologically incorporated. Here, we report the synthesis of a series of tripeptide thioesters as mutasynthons containing the native sequence with a dehydroalanine (Dha) Michael acceptor attached to a sarcosine (Sar) and derivatives. Chemical synthesis of the native sequence ᴅ-Ala-Dha-Sar thioester required revision of the sequential peptide synthesis into a convergent strategy where the thioester with sarcosine was formed before coupling to the Dha-containing dipeptide.
CitationBeilstein J Org Chem. 2019 Dec 5;15:2922-2929. doi: 10.3762/bjoc.15.286. eCollection 2019.
AffiliationBRICS, Braunschweiger Zentrum für Systembiologie, Rebenring 56,38106 Braunschweig, Germany.
The following license files are associated with this item:
- Creative Commons
Except where otherwise noted, this item's license is described as Attribution-NonCommercial-ShareAlike 4.0 International
- Biosynthesis and Heterologous Production of Argyrins.
- Authors: Pogorevc D, Tang Y, Hoffmann M, Zipf G, Bernauer HS, Popoff A, Steinmetz H, Wenzel SC
- Issue date: 2019 May 17
- Mutation in elongation factor G confers resistance to the antibiotic argyrin in the opportunistic pathogen Pseudomonas aeruginosa.
- Authors: Bielecki P, Lukat P, Hüsecken K, Dötsch A, Steinmetz H, Hartmann RW, Müller R, Häussler S
- Issue date: 2012 Nov 5
- Identification of elongation factor G as the conserved cellular target of argyrin B.
- Authors: Nyfeler B, Hoepfner D, Palestrant D, Kirby CA, Whitehead L, Yu R, Deng G, Caughlan RE, Woods AL, Jones AK, Barnes SW, Walker JR, Gaulis S, Hauy E, Brachmann SM, Krastel P, Studer C, Riedl R, Estoppey D, Aust T, Movva NR, Wang Z, Salcius M, Michaud GA, McAllister G, Murphy LO, Tallarico JA, Wilson CJ, Dean CR
- Issue date: 2012
- Determinants of Antibacterial Spectrum and Resistance Potential of the Elongation Factor G Inhibitor Argyrin B in Key Gram-Negative Pathogens.
- Authors: Jones AK, Woods AL, Takeoka KT, Shen X, Wei JR, Caughlan RE, Dean CR
- Issue date: 2017 Apr
- Total synthesis approaches to natural product derivatives based on the combination of chemical synthesis and metabolic engineering.
- Authors: Kirschning A, Taft F, Knobloch T
- Issue date: 2007 Oct 21