Protective Effects of L- and D-Carnosine on R-Crystallin Amyloid Fibril Formation: Implications for Cataract Disease (Articolo in rivista)

Type
Label
  • Protective Effects of L- and D-Carnosine on R-Crystallin Amyloid Fibril Formation: Implications for Cataract Disease (Articolo in rivista) (literal)
Anno
  • 2009-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1021/bi900343n (literal)
Alternative label
  • F. Attanasio, S. Cataldo, S. Fisichella, S. Nicoletti, V.G. Nicoletti, B. Pignataro, A. Savarino, E. Rizzarelli. (2009)
    Protective Effects of L- and D-Carnosine on R-Crystallin Amyloid Fibril Formation: Implications for Cataract Disease
    in Biochemistry (Easton)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • F. Attanasio, S. Cataldo, S. Fisichella, S. Nicoletti, V.G. Nicoletti, B. Pignataro, A. Savarino, E. Rizzarelli. (literal)
Pagina inizio
  • 6522 (literal)
Pagina fine
  • 6531 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 48 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • F. Attanasio: Institute of Biostructures and Bioimaging (IBB), CNR, 95125 Catania, Italy, S. Cataldo, B. Pignataro:Dipartimento di Chimica Fisica \"F. Accascina\", Università di Palermo, 90128 Palermo, Italy, S. Fisichella, S. Nicoletti, V.G. Nicoletti, A. Savarino, E. Rizzarelli: Department of Chemical Sciences, University of Catania, 95125 Catania, Italy, and National Institute of Biostructures and Biosystems, 95125 Catania, Italy (literal)
Titolo
  • Protective Effects of L- and D-Carnosine on R-Crystallin Amyloid Fibril Formation: Implications for Cataract Disease (literal)
Abstract
  • Mildly denaturing conditions induce bovine ?-crystallin, the major structural lens protein, to self-assemble into fibrillar structures in vitro. The natural dipeptide L-carnosine has been shown to have potential protective and therapeutic significance in many diseases. Carnosine derivatives have been proposed as potent agents for ophthalmic therapies of senile cataracts and diabetic ocular complications. Here we report the inhibitory effect induced by the peptide (L- and D-enantiomeric form) on ?-crystallin fibrillation and the almost complete restoration of the chaperone activity lost after denaturant and/or heat stress. Scanning force microscopy (SFM), thioflavin T, and a turbidimetry assay have been used to determine the morphology of ?-crystallin aggregates in the presence and absence of carnosine. DSC and a near-UV CD assay evidenced that the structural precursors of amyloid fibrils are polypeptide chain segments that lack stable structural elements. Moreover, we have found a disassembling effect of carnosine on ?-crystallin amyloid fibrils. Finally, we show the ability of carnosine to restore most of the lens transparency in organ-cultured rat lenses exposed to similar denaturing conditions that were used for the in vitro experiments. © 2009 American Chemical Society. (literal)
Prodotto di
Autore CNR
Insieme di parole chiave

Incoming links:


Prodotto
Autore CNR di
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
Insieme di parole chiave di
data.CNR.it