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Cyclic peptides bearing a side-chain tail: A tool to model the structure and reactivity of protein zinc sites.

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  • معلومة اضافية
    • Contributors:
      Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249); Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes 2016-2019 (UGA 2016-2019 )-Institut de Recherche Interdisciplinaire de Grenoble (IRIG); Direction de Recherche Fondamentale (CEA) (DRF (CEA)); Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)); Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA); Département de Chimie Moléculaire (DCM); Université Joseph Fourier - Grenoble 1 (UJF)-Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS); ANR-06-JCJC-0018,ZINCCYS,Implications des sites zinc-cystéinates dans le stress peroxydique: approche mécanistique par des modèles peptidiques(2006)
    • بيانات النشر:
      CCSD
      Wiley-VCH Verlag
    • الموضوع:
      2008
    • Collection:
      HAL-CEA (Commissariat à l'énergie atomique et aux énergies alternatives)
    • نبذة مختصرة :
      International audience ; A new peptide design has been introduced to model the tetracysteinate zinc sites involving CXXC motifs present in beta-hairpins. It is based on a cyclic peptide incorporating one CXXC motif in addition to a variable CXC motif in a linear chain grafted onto the cycle via a glutamate or a lysine side chain. This 20-amino acid design has been used to model the Zn(Cys)4 sites of the heat shock protein Hsp33. TheZn2+ and Co2+ complexes were characterized by UV/vis, CD and NMR spectroscopy. The structures of two metallated peptides were solved by NMR. An excellent similarly was achieved between the model peptide and the target protein, both at the metal binding site and in the surrounding hydrogen bond network. Preliminary reactivity studies toward H2O2 are reported and show that the best model fit the kinetics observed for Hsp33.
    • Relation:
      info:eu-repo/semantics/altIdentifier/pmid/18651686; PUBMED: 18651686
    • الرقم المعرف:
      10.1002/anie.200800677
    • الدخول الالكتروني :
      https://hal.science/hal-00373744
      https://hal.science/hal-00373744v1/document
      https://hal.science/hal-00373744v1/file/seneque_cyclic_peptides.pdf
      https://doi.org/10.1002/anie.200800677
    • Rights:
      info:eu-repo/semantics/OpenAccess
    • الرقم المعرف:
      edsbas.7488AD92