bc050299g_si_001.pdf (2.67 MB)
Interaction of C60-Fullerene and Carboxyfullerene with Proteins: Docking and Binding Site Alignment
journal contribution
posted on 2006-03-15, 00:00 authored by Hadar Benyamini, Alexandra Shulman-Peleg, Haim J. Wolfson, Bogdan Belgorodsky, Ludmila Fadeev, Michael GozinThe unique properties of fullerenes have raised the interest of using them for biomedical applications. Within this
framework, the interactions of fullerenes with proteins have been an exciting research target, yet little is known
about how native proteins can bind fullerenes, and what is the nature of these interactions. Moreover, though
some proteins have been shown to interact with fullerenes, up to date, no crystal structure of such complexes was
obtained. Here we report docking studies aimed at examining the interactions of fullerene in two forms (C60
nonsubstituted fullerene and carboxyfullerene) with four proteins that are known to bind fullerene derivatives:
HIV protease, fullerene-specific antibody, human serum albumin, and bovine serum albumin. Our work provides
docking models with detailed binding pockets information, which closely match available experimental data. We
further compare the predicted binding sites using a novel multiple binding site alignment method. A high similarity
between the physicochemical properties and surface geometry was found for fullerene's binding sites of HIV
protease and the human and bovine serum albumins.