Unser 10. Leibniz Plant Biochemistry Symposium am 7. und 8. Mai war ein großer Erfolg. Thematisch ging es in diesem Jahr um neue Methoden und Forschungsansätze der Naturstoffchemie. Die exzellenten Vorträge über Wirkstoffe…
Omanische Heilpflanze im Fokus der Phytochemie IPB-Wissenschaftler und Partner aus Dhofar haben jüngst die omanische Heilpflanze Terminalia dhofarica unter die phytochemische Lupe genommen. Die Pflanze ist reich an…
Geschmack ist vorhersagbar: Mit FlavorMiner. FlavorMiner heißt das Tool, das IPB-Chemiker und Partner aus Kolumbien jüngst entwickelt haben. Das Programm kann, basierend auf maschinellem Lernen (KI), anhand der…
Corrêa dos Santos, C. H.; Geraldo de Carvalho, M.; Laub, A.; Franke, K.; Wessjohann, L.;UHPLC-ESI-Orbitrap-HR-MS analysis of cyclopeptide alkaloids from Ziziphus joazeiroNat. Prod. Commun.161-13(2021)DOI: 10.1177/1934578x211054955
Ziziphus joazeiro Mart., popularly known as “juazeiro”, is a tree widely found in the northeast of Brazil. It is commonly used as an anti-inflammatory, antibacterial, antifungal, and analgesic agent. The stem extract exhibited, beside cytotoxic properties, substantial activity against the Gram-negative bacterium Allivibrio fischeri. UHPLC-ESI-Orbitrap-HR-MS analysis of the alkaloidal fraction of the crude methanolic stem extract of this species enabled the detection and putative identification of sixteen cyclopeptide alkaloids (CPAs), including four possibly new structures. According to the MS2 fragmentation analysis, from the sixteen identified CPAs, three possess a type-Ia1, one a type-Ia2, and twelve a type-Ib cyclopeptide alkaloid core. The structures of paliurine-C and -D were supported by NMR data.
Publikation
Ricardo, M. G.; Moya, C. G.; Pérez, C. S.; Porzel, A.; Wessjohann, L. A.; Rivera, D. G.;Improved Stability and Tunable Functionalization of Parallel β‐Sheets via Multicomponent N‐Alkylation of the Turn MoietyAngew. Chem.132265-269(2020)DOI: 10.1002/ange.201912095
In contrast to the myriad of methods available to produce α‐helices and antiparallel β‐sheets in synthetic peptides, just a few are known for the construction of stable, non‐cyclic parallel β‐sheets. Herein, we report an efficient on‐resin approach for the assembly of parallel β‐sheet peptides in which the N‐alkylated turn moiety enhances the stability and gives access to a variety of functionalizations without modifying the parallel strands. The key synthetic step of this strategy is the multicomponent construction of an N‐alkylated turn using the Ugi reaction on varied isocyano‐resins. This four‐component process assembles the orthogonally protected turn fragment and incorporates handles serving for labeling/conjugation purposes or for reducing peptide aggregation. NMR and circular dichroism analyses confirm the better‐structured and more stable parallel β‐sheets in the N‐alkylated peptides compared to the non‐functionalized variants.
Publikation
Ricardo, M. G.; Llanes, D.; Wessjohann, L. A.; Rivera, D. G.;Introducing the Petasis Reaction for Late-Stage Multicomponent Diversification, Labeling, and Stapling of PeptidesAngew. Chem.1312726-2730(2019)DOI: 10.1002/ange.201812620
For the first time, the Petasis (borono‐Mannich) reaction is employed for the multicomponent labeling and stapling of peptides. The report includes the solid‐phase derivatization of peptides at the N‐terminus, Lys, and Nϵ‐MeLys side‐chains by an on‐resin Petasis reaction with variation of the carbonyl and boronic acid components. Peptides were simultaneously functionalized with aryl/vinyl substituents bearing fluorescent/affinity tags and oxo components such as dihydroxyacetone, glyceraldehyde, glyoxylic acid, and aldoses, thus encompassing a powerful complexity‐generating approach without changing the charge of the peptides. The multicomponent stapling was conducted in solution by linking Nϵ‐MeLys or Orn side‐chains, positioned at i, i+7 and i, i+4, with aryl tethers, while hydroxy carbonyl moieties were introduced as exocyclic fragments. The good efficiency and diversity oriented character of these methods show prospects for peptide drug discovery and chemical biology.
Publikation
Püllmann, P.; Weissenborn, M. J.;Pilzliche Peroxygenasen: der Schlüssel zu C-H-Hydroxylierungen und mehr?BIOspektrum25572-574(2019)DOI: 10.1007/s12268-019-1090-2
Fungal peroxygenases represent an exciting new enzyme class for stereo-selective hydroxylation reactions. They are capable of the oxyfunctionalisation of a large, diverse scope of substrates including alkanes and steroids as well as the heteroatoms sulfur and nitrogen. The outstanding activities and stabilities as well as their reliance on hydrogen peroxide as co-substrate renders it a highly interesting biocatalyst.