N-terminal deletion affects catalytic activity of saporin toxin. (Articolo in rivista)

Type
Label
  • N-terminal deletion affects catalytic activity of saporin toxin. (Articolo in rivista) (literal)
Anno
  • 2006-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1002/jcb.20845 (literal)
Alternative label
  • Bonini F., Traini R., Comper F., Fracasso G., Tomazzolli R., Dalla Serra M., Colombatti M. (2006)
    N-terminal deletion affects catalytic activity of saporin toxin.
    in Journal of cellular biochemistry (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Bonini F., Traini R., Comper F., Fracasso G., Tomazzolli R., Dalla Serra M., Colombatti M. (literal)
Pagina inizio
  • 1130 (literal)
Pagina fine
  • 1139 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 98 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Department of Pathology, Section of Immunology, University of Verona, Italy ITC & CNR, Institute of Biophysics, Section of Trento, Povo (Trento), Italy (literal)
Titolo
  • N-terminal deletion affects catalytic activity of saporin toxin. (literal)
Abstract
  • Single-chain ribosome inactivating proteins (RIPs) are cytotoxic components of macromolecular pharmaceutics for immunotherapy of cancer and other human diseases. Saporin belongs to a family of single-chain RIPs sharing sequence and structure homology. In a preliminary attempt to define an active saporin polypeptide of minimum size we have generated proteins with deletions at the N-terminus and at the C-terminus. An N-terminal (sapDelta1-20) deletion mutant of saporin displayed defective catalytic activity, drastically reduced cytotoxicity but increased ability to interact with liposomes inducing their permeabilization at low pH. A C-terminal (sapDelta239-253) deletion mutant showed instead a moderate reduction in cytotoxic activity. A substantial alteration of secondary structure was evidenced by Fourier transformed infrared spectroscopy (FTIR) in the sapDelta1-20 mutant. It can be hypothesized that the defective functions of sapDelta1-20 are due to alterations of its spatial configuration. (literal)
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Autore CNR

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