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  Photomodulation of the redox and folding adjuvant properties of bis(cysteinyl) peptides

Cabrele, C., Cattani-Scholz, A., Renner, C., Behrendt, R., Oesterhelt, D., & Moroder, L. (2002). Photomodulation of the redox and folding adjuvant properties of bis(cysteinyl) peptides. European Journal of Organic Chemistry, (13), 2144-2150.

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Genre: Zeitschriftenartikel
Alternativer Titel : Eur. J. Org. Chem.

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 Urheber:
Cabrele, C.1, Autor           
Cattani-Scholz, A.1, Autor           
Renner, C.1, Autor           
Behrendt, R.1, Autor           
Oesterhelt, D.2, Autor           
Moroder, L.1, Autor           
Affiliations:
1Moroder, Luis / Bioorganic Chemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565160              
2Oesterhelt, Dieter / Membrane Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565164              

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Schlagwörter: azobenzene; peptides; folding adjuvants; photomodulation; redox chemistry
 Zusammenfassung: The octapeptide [134-141] related to the active-site fragment of thioredoxin reductase, in which three residues outside the characteristic Cys-Xaa-Yaa-Cys motif of thiol/disulfide oxidoreductases were replaced by lysines, was head-to-tail- cyclized by using the suitably functionalized (4- aminomethyl)phenylazobenzoic acid (AMPB). The resulting monocyclic and disulfide-bridged bicyclic compounds underwent light-induced cis/trans isomerization in a fully reversible manner, with well-defined conformational transitions as a result of the strong differences in the molecular geometries of the trans and cis-azobenzene units. Correspondingly, the trans and cis forms of the cyclic bis(cysteinyl)-AMPB peptide were characterized by significantly differentiated redox potentials, which were exploited to catalyze the oxidative refolding of reduced RNase A with distinct efficiencies. The experimental results showed that the incorporation of the azobenzene moiety into conformationally restricted bis(cysteinyl) peptide systems provided folding adjuvants that photocontrolled the rates of oxidative protein folding.

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Sprache(n): eng - English
 Datum: 2002-07
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: eDoc: 41358
ISI: 000176718200017
 Art des Abschluß: -

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Titel: European Journal of Organic Chemistry
  Alternativer Titel : Eur. J. Org. Chem.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: (13) Artikelnummer: - Start- / Endseite: 2144 - 2150 Identifikator: ISSN: 1434-193X