Model simulations of the adsorption of statherin to solid surfaces: Effects of surface charge and hydrophobicity

DSpace Repository

Model simulations of the adsorption of statherin to solid surfaces: Effects of surface charge and hydrophobicity

Show full item record

Files for download

Find Full text There are no files associated with this item..

Facebook

Simple item record

Publication Article, peer reviewed scientific
Title Model simulations of the adsorption of statherin to solid surfaces: Effects of surface charge and hydrophobicity
Author(s) Skepö, Marie
Date 2008-11
English abstract
The structural properties of the salivary protein statherin upon adsorption have been examined using a coarse-grained model and Monte Carlo simulation. A simple model system with focus on electrostatic interactions and short-ranged attractions among the uncharged amino acids has been used. To mimic hydrophobically modified surfaces, an extra short-ranged interaction was implemented between the amino acids and the surface. It has been shown that the adsorption and the thickness of the adsorbed layer are determined by (i) the affinity for the surface, i.e., denser layer with an extrashort-ranged potential, and (ii) the distribution of the charges along the chain. If all the amino acids have a high affinity for the surface, the protein adsorbs in a train conformation, if the surface is negatively charged the protein adsorbs in a tail-train conformation, whereas if the surface is positively charged the protein adsorbs in a loop conformation. The latter gives rise to a more confined adsorbed layer. ©2008 American Institute of Physics
Host/Issue Journal of Chemical Physics;18
Volume 129
Pages 185101
Language eng (iso)
Subject(s) Sciences
Research Subject Categories::NATURAL SCIENCES
Handle http://hdl.handle.net/2043/6829 (link to this page)

This item appears in the following Collection(s)

Show full item record

Search


Browse

My Account

Statistics