title: Baiting proteins with C60.
abstract: About 20 proteins are known to modify their activity upon interaction with C60. Their structures are present in a database that includes more than 1200 protein structures selected as possible targets for drugs and to represent the entire Protein Data Bank. The set was examined with an algorithm that appraises quantitatively the interaction of C60 and the surface of each protein. The redundancy of the set allows to establish the predictive power of the approach that finds explicitly the most probable site where C60 docks on each protein. About 80% of the known fullerene binding proteins fall in the top 10% of scorers. The close match between the model and experiments vouches for the accuracy of the model and validates its predictions. The sites of docking are shown and discussed in view of the existing experimental data available for protein-C60 interaction. A closer exam of the 10 top scorers is discussed in detail. New proteins that can interact with C60 are identified and discussed for possible future applications as drug targets and fullerene derivatives bioconjugate materials.
authors.affiliation: Dipartimento di Chimica "G. Ciamician", Universita' di Bologna, V. F. Selmi 2, 40126 Bologna, Italy. matteo.calvaresi@studio.unibo.it
authors.forename: Matteo
authors.initials: M
authors.lastname: Calvaresi
authors.forename: Francesco
authors.initials: F
authors.lastname: Zerbetto
mesh_terms: D000818:Animals; D001665:Binding Sites; D002417:Cattle; D003198:Computer Simulation; D018360:Crystallography, X-Ray; D030562:Databases, Protein; D037741:Fullerenes / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D051379:Mice; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D051381:Rats
chemical_list: D037741:Fullerenes; D011506:Proteins; C069837:fullerene C60