Abstract
Thermolysin, α-chymotrypsin, and papain were used as biocatalysts for the coupling of several carboxyl components to silica-supported leucine amide as a nucleophile. A spacer length of 21 covalent bonds corresponding to 7 amino acid residues was required for successful coupling. This approach offers the possibility of using proteases for racemization-free segment condensations on insoluble polymeric supports.
Zusammenfassung
Thermolysin, α-Chymotrypsin und Papain wurden als Biokatalysatoren für die Kupplung verschiedener Carboxylkomponenten an kieselgel-gebundenes Leucinamid als Nucleophil eingesetzt. Für erfolgreiche Kupplungen war eine Spacerlänge von 21 kovalenten Bindungen entsprechend 7 Aminosäureresten erforderlich. Diese Synthesevariante eröffnet die Möglichkeit, racemisierungsfreie Segmentkondensationen an unlöslichen polymeren Trägern mit Hilfe von Proteasen durchzuführen.
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Könnecke, A., Dettlaff, S. & Jakubke, HD. Model studies on the utility of nucleophiles bound to insoluble supports for enzymatic peptide synthesis. Monatsh Chem 113, 331–337 (1982). https://doi.org/10.1007/BF00799560
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DOI: https://doi.org/10.1007/BF00799560