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

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons77832

Cabrele,  C.
Moroder, Luis / Bioorganic Chemistry, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons77839

Cattani-Scholz,  A.
Moroder, Luis / Bioorganic Chemistry, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78560

Renner,  C.
Moroder, Luis / Bioorganic Chemistry, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons77731

Behrendt,  R.
Moroder, Luis / Bioorganic Chemistry, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78468

Oesterhelt,  D.
Oesterhelt, Dieter / Membrane Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78419

Moroder,  L.
Moroder, Luis / Bioorganic Chemistry, Max Planck Institute of Biochemistry, Max Planck Society;

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Zitation

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.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0010-6EDC-4
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.