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Chemoenzymatic synthesis of lipidated peptides

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons98735

Waldmann,  Herbert
Abt. IV: Chemische Biologie, Max Planck Institute of Molecular Physiology, Max Planck Society;

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Zitation

Kadereit, D., & Waldmann, H. (2000). Chemoenzymatic synthesis of lipidated peptides. MONATSHEFTE FUR CHEMIE, 131(6), 571-584. doi:10.1007/s007060070087.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0014-6F11-3
Zusammenfassung
This review highlights the use of enzymatic protecting group techniques in the synthesis of lipidated peptides. Lipidated proteins play key roles in signal transduction processes. Moreover, structurally well-defined peptides containing the characteristic linkage region of the peptide backbone with the lipid can provide valuable tools for the study of biological phenomena associated with these protein conjugates. The multifunctionality and pronounced lability towards acids and bases of such compounds render their synthesis a formidable challenge. However, the recent development of enzymatic protection groups provides an efficient access to these sensitive and biologically relevant peptide conjugates under particular mild conditions and with high selectivity.