TY - JOUR
T1 - Interaction of C60-fullerene and carboxyfullerene with proteins
T2 - Docking and binding site alignment
AU - Benyamini, Hadar
AU - Shulman-Peleg, Alexandra
AU - Wolfson, Haim J.
AU - Belgorodsky, Bogdan
AU - Fadeev, Ludmila
AU - Gozin, Michael
PY - 2006
Y1 - 2006
N2 - The 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.
AB - The 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.
UR - http://www.scopus.com/inward/record.url?scp=33645462298&partnerID=8YFLogxK
U2 - 10.1021/bc050299g
DO - 10.1021/bc050299g
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AN - SCOPUS:33645462298
SN - 1043-1802
VL - 17
SP - 378
EP - 386
JO - Bioconjugate Chemistry
JF - Bioconjugate Chemistry
IS - 2
ER -