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  Chemoenzymatic synthesis of lipidated peptides

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

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 Urheber:
Kadereit, D1, Autor
Waldmann, Herbert2, Autor           
Affiliations:
1external, ou_persistent22              
2Abt. IV: Chemische Biologie, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753290              

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Schlagwörter: ALLYLIC PROTECTING GROUPS; ORGANIC-SYNTHESIS; RAS LIPOPEPTIDES; N-RAS; PROTEINS; ENVIRONMENT; ACYLATION; ANALOGS; BINDING; Chemistry; lipidated peptides; chemoenzymatic Synthesis; enzyme-labile protecting groups; Ras proteins;
 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.

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Sprache(n): eng - English
 Datum: 2000-06
 Publikationsstatus: Erschienen
 Seiten: 14
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Identifikatoren: ISI: 000088229100004
DOI: 10.1007/s007060070087
 Art des Abschluß: -

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Titel: MONATSHEFTE FUR CHEMIE
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: Wien : SPRINGER-VERLAG
Seiten: - Band / Heft: 131 (6) Artikelnummer: - Start- / Endseite: 571 - 584 Identifikator: ISSN: 0026-9247