Proline-Glutamate Chimeras in Isopeptides., Synthesis and Biological Evaluation of Conformationally Restricted Glutathione Analogues (Articolo in rivista)

Type

• Articolo in rivista (Classe)
• Prodotto della ricerca (Classe)

Label

• Proline-Glutamate Chimeras in Isopeptides., Synthesis and Biological Evaluation of Conformationally Restricted Glutathione Analogues (Articolo in rivista) (literal)

Anno

• 2003-01-01T00:00:00+01:00 (literal)

Alternative label

• Paglialunga Paradisi M., Mollica A., Cacciatore I., Di Stefano A., Pinnen F., Caccuri A.M., Ricci G., Duprè S., Spirito A., Lucente G. (2003)
  Proline-Glutamate Chimeras in Isopeptides., Synthesis and Biological Evaluation of Conformationally Restricted Glutathione Analogues
  in Bioorganic & medicinal chemistry (Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Paglialunga Paradisi M., Mollica A., Cacciatore I., Di Stefano A., Pinnen F., Caccuri A.M., Ricci G., Duprè S., Spirito A., Lucente G. (literal)

Pagina inizio

• 1677 (literal)

Pagina fine

• 1683 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 11 (literal)

Rivista

• Bioorganic & medicinal chemistry (Rivista)

Note

• ISI Web of Science (WOS) (literal)

Titolo

• Proline-Glutamate Chimeras in Isopeptides., Synthesis and Biological Evaluation of Conformationally Restricted Glutathione Analogues (literal)

Abstract

• The two novel diastereoisomeric glutathione analogues 1 and 2 have been designed and synthesized by replacing the native y-glutamylic moiety with the conformational rigid skeleton of cis- or trans-4-carboxy-L-proline residue. Both analogues have been obtained by following the solution phase peptide chemistry methodologies and final reduction of the corresponding disulfide forms 13 and 14. The two analogues 1 and 2 have been tested towards y-glutamyltranspeptidase (y-GT)and human glutathione S-transferase (hGST P1-1). Both analogues 1 and 2 are completely resistant to enzymatic degradation by y-GT. The S-transferase utilizes the analogue 2 as a good substrate while is unable to bind the analogue 1. 2003 Elsevier Science Ltd. All rights reserved. (literal)

Prodotto di

• Institute of biomolecular chemistry (ICB) (Istituto)

Incoming links:

Prodotto

• Institute of biomolecular chemistry (ICB) (Istituto)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Bioorganic & medicinal chemistry (Rivista)