Prion diseases, also known as transmissible spongiform encephalopathies (TSE), are fatal neurodegenerative disorders of the central nervous system. The main molecular mechanism underlining TSE is based on the aberrant misfolding of the cellular form of the prion protein (PrPC) into its pathological counterpart denominated PrPSc. To date there are no identified therapies. One therapeutic strategy against this disease is focused on the stabilization of the PrPC in order to prevent its conversion to PrPSc . Designing ligands targeting PrPC with a high binding affinity might augment its stability and prevent its misfolding. Here, we have set-up a computational protocol aiming at addressing this issue.
DESIGN OF LIGANDS WITH A HIGH AFFINITY TO PrPC / A. Kranjc; S. Bongarzone; G. Chiriano; G. Rossetti; X. Biarnés; A. Cavalli; M.L. Bolognesi; M. Roberti; G. Legname; P. Carloni. - STAMPA. - (2008), pp. 34-34. (Intervento presentato al convegno International Workshop HUMAN and ANIMAL TSE tenutosi a Grado, Italy nel 26-28 Giugno 2008).
DESIGN OF LIGANDS WITH A HIGH AFFINITY TO PrPC
CAVALLI, ANDREA;BOLOGNESI, MARIA LAURA;ROBERTI, MARINELLA;
2008
Abstract
Prion diseases, also known as transmissible spongiform encephalopathies (TSE), are fatal neurodegenerative disorders of the central nervous system. The main molecular mechanism underlining TSE is based on the aberrant misfolding of the cellular form of the prion protein (PrPC) into its pathological counterpart denominated PrPSc. To date there are no identified therapies. One therapeutic strategy against this disease is focused on the stabilization of the PrPC in order to prevent its conversion to PrPSc . Designing ligands targeting PrPC with a high binding affinity might augment its stability and prevent its misfolding. Here, we have set-up a computational protocol aiming at addressing this issue.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
