Ordering in a fibrinogen layer

TL;DR

This study investigates the ordering of fibrinogen protein layers using simulations to understand how orientation affects their structural and kinetic properties, providing insights into their physicochemical behavior.

Contribution

We introduce a simulation approach with non-uniform orientation distribution to analyze fibrinogen layer ordering and its impact on coverage and adsorption kinetics.

Findings

Coverage ratio depends on orientational order

Autocorrelation function reveals spatial structure

Available Surface Function varies with order level

Abstract

Ordered protein layers are the subject of active biomedical research for their usually interesting physicochemical properties, e.g. permeability, stiffness and pours structure. In presented work, we focused on layers build of fibrinogen molecules characterised by strong shape anisotropy. Using Random Sequential Adsorption (RSA) method, we simulated adsorption process in which the orientation of adsorbate was described by a non-uniform probability distribution. Thus obtained covering layers had different level of global orientational ordering. This allowed us to find dependence between main properties of layers, such as maximal random coverage ratio, and order parameter. For better description and deeper understanding of obtained structures, the autocorrelation function as well as distribution of uncovered space were determined. Additionally, we calculated the Available Surface Function (ASF), which is essential for determining adsorption kinetics.