Modellstudien zur Anwendbarkeit von an unlösliche Träger gebundenen Nucleophilen für die enzymatische Peptidsynthese

The stereospecific formation of peptide bonds under mild conditions and without side reactions is still a formidable task in peptide synthesis. One approach that springs to mind, namely the use of the naturally occurring catalyst involved in the biosynthesis of proteins, the ribosomal peptidyl transferase, cannot be realized in practice. The fact, however, that the natural cleavage of proteins is carried out by other enzymes, namely the proteases, together with the reversibility of these cleavage reactions in principle, has led to an interesting synthetic concept. Proteases normally catalyze the enzymatic degradation of proteins and peptides by hydrolytic cleavage of the peptide bond in an exergonic reaction. The use of physicochemical principles in order to influence the equilibrium, the concentration of products, and the kinetic parameters of the reaction results in the successful application of the catalytic properties of proteases to peptide synthesis. The purpose of this review is to describe and summarize the methods used in such approaches and to attempt a systematic categorization. The principles are applied to the synthesis of such practically relevant products as aspartame and human insulin.

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ChemInform Abstract: MODEL STUDIES ON THE UTILITY OF NUCLEOPHILES BOUND TO INSOLUBLE SUPPORTS FOR ENZYMIC PEPTIDE SYNTHESIS

Koennecke¹,

Dettlaff²,

Jakubke³

1982

Chemischer Informationsdienst

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Modellstudien zur Anwendbarkeit von an unlösliche Träger gebundenen Nucleophilen für die enzymatische Peptidsynthese

Cited by 7 publications

References 15 publications

Grundprinzipien der proteasekatalysierten Knüpfung der Peptidbindung

Grundprinzipien der proteasekatalysierten Knüpfung der Peptidbindung

Basic Principles of Protease‐Catalyzed Peptide Bond Formation

ChemInform Abstract: MODEL STUDIES ON THE UTILITY OF NUCLEOPHILES BOUND TO INSOLUBLE SUPPORTS FOR ENZYMIC PEPTIDE SYNTHESIS

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