Abstract
The ability of proteins to bind selectively to different kinds of solid surfaces is widely used in advanced technologies in medicine, pharmacy, nanodevices and bioengineering. However, experimental data on the interfacial behavior of proteins is limited and our knowledge of the driving forces for protein-solid surface binding is still very poor. The present study is aimed at building a computational model for understanding and predicting the chemical and physical properties of protein-solid surface systems.As a test example, adsorption of the BLIP (beta-lactamase inhibitor protein) protein fused with different homotripeptides to the gold surface is explored. The computational algorithm is based on Brownian dynamics simulations of a protein in the presence of a metal surface with interactions described by electrostatic, Lennard-Jones (LJ), and desolvation energy terms. The interatomic LJ potential describes both the van der Waals and the chemical interaction between amino acids and the gold surface with parameters derived from ab initio calculations and experimental data. The desolvation term includes protein desolvation as well as surface water desorption effects. The results of the computer simulations are compared with the experimentally observed binding characteristics of the systems under consideration.We thank our partners in the Prosurf project, in particular G. Schreiber and D. Reichmann for sharing experimental data, K. Gottschak and M. Hofling for caring out MD simulations, and S. Corni and F. Iori for providing force field parameters for peptides on the gold surface.This project is carried out with financial support from KTS Klaus Tschira Foundation gGmbH and the European Community.
Published Version
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call