Proc. Electrochem. Soc. Abstract
Abstract
Since the complementary relationship between fullerene
C60
and the cavity of Human Immunodeficiency Virus Protease (HIVP)
was first described, C60-based
HIVP inhibitors have attracted the attention of the research community.
In the present study, molecular dynamics (MD) simulations of complexes
of HIVP with
C60 and with a biologically active
derivative
were performed in order to investigate the
ability of C60 to localize
in the enzyme cavity near the active site. Qualitative and quantitative
analyses based on these data allow some tentative conclusions to be
drawn about the nature of the interactions of functionalized fullerenes
with HIVP.
In particular, it was found that the
activity of the inhibitors correlated with the value of
Rasp-asp, the distance between
C-gamma carbons of ASP25 and ASP125 in the various complexes.