title: Sequential adsorption of proteins and the surface modification of biomaterials: a molecular dynamics study.
abstract: The sequential adsorption of two proteins of the same or of an unlike nature on a heterogeneous hydrophobic surface is investigated through atomistic molecular dynamics simulations. By modeling two real protein fragments having a different secondary structure (alpha-helices or beta-sheets) on a graphite surface, the pre-adsorbed polypeptides are shown to modify the hydropathy of this substrate. Therefore, the graphite surface modified by the first adsorbed protein becomes more similar to a hydrophilic one in terms of both the interaction energy and the size of the second protein after the possible surface spreading.
authors.affiliation: Dipartimento di Chimica, Materiali e Ingegneria Chimica G. Natta, Politecnico, via L. Mancinelli 7, 20131, Milano, Italy. giuseppina.raffaini@polimi.it
authors.forename: Giuseppina
authors.initials: G
authors.lastname: Raffaini
authors.forename: Fabio
authors.initials: F
authors.lastname: Ganazzoli
mesh_terms: D000327:Adsorption; D001665:Binding Sites; D001672:Biocompatible Materials / Q000737:chemistry*; D003198:Computer Simulation; D003460:Crystallization / Q000379:methods; D007700:Kinetics; D008956:Models, Chemical; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D013499:Surface Properties
chemical_list: D001672:Biocompatible Materials; D011506:Proteins