Modelling of binding modes and inhibition mechanism of some natural ligands of farnesyl transferase using molecular docking
Articolo
Data di Pubblicazione:
2002
Citazione:
Modelling of binding modes and inhibition mechanism of some natural ligands of farnesyl transferase using molecular docking / A. Pedretti, L. Villa, G. Vistoli. - In: JOURNAL OF MEDICINAL CHEMISTRY. - ISSN 0022-2623. - 45:7(2002 Feb 21), pp. 1460-1465.
Abstract:
Several natural inhibitors of farnesyl transferase have been reported in the literature: some
compounds are competitive with farnesyl pyrophosphate (FPP), whereas other ones are
competitive with Ras proteins, even though it is usually hard to highlight their inhibition
mechanism, which is still unknown for several natural compounds. The aim of this work is to
show that the molecular docking analysis can be successfully used to underline the inhibition
mechanism of these natural compounds. First, the selected compounds were subjected to a
detailed docking analysis, by means of BioDock, a program able to reveal the most likely binding
mode for each ligand. By comparing these results with the binding sites for the natural
substrates, earlier determined, it was possible to highlight the site specificity and the inhibition
mechanism of the selected compounds. In addition, it is possible to relate the binding mode of
these molecules with their lipole values, which is appreciably less for peptidomimetics than
for FPP mimetic and reveals a straightforward method to predict and to understand the
inhibition mechanism of these natural derivatives.
Tipologia IRIS:
01 - Articolo su periodico
Elenco autori:
A. Pedretti, L. Villa, G. Vistoli
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