Picture of DNA strand

Pioneering chemical biology & medicinal chemistry through Open Access research...

Strathprints makes available scholarly Open Access content by researchers in the Department of Pure & Applied Chemistry, based within the Faculty of Science.

Research here spans a wide range of topics from analytical chemistry to materials science, and from biological chemistry to theoretical chemistry. The specific work in chemical biology and medicinal chemistry, as an example, encompasses pioneering techniques in synthesis, bioinformatics, nucleic acid chemistry, amino acid chemistry, heterocyclic chemistry, biophysical chemistry and NMR spectroscopy.

Explore the Open Access research of the Department of Pure & Applied Chemistry. Or explore all of Strathclyde's Open Access research...

Fibronectin module FNIII9 adsorption at contrasting solid model surfaces studied by atomistic molecular dynamics

Kubiak-Ossowska, Karina and Mulheran, Paul A. and Nowak, Wieslaw (2014) Fibronectin module FNIII9 adsorption at contrasting solid model surfaces studied by atomistic molecular dynamics. Journal of Physical Chemistry B, 118 (33). pp. 9900-9908. ISSN 1520-6106

[img]
Preview
Text (Kubiak-Ossowska-etal-JOPCB-2015-Fibronectin-module-FNIII9-adsorption-at-contrasting)
Kubiak_Ossowska_etal_JOPCB_2015_Fibronectin_module_FNIII9_adsorption_at_contrasting.pdf
Accepted Author Manuscript

Download (5MB) | Preview

Abstract

The mechanism of human fibronectin adhesion synergy region (known as integrin binding region) in repeat 9 (FNIII9) domain adsorption at pH 7 onto various and contrasting model surfaces has been studied using atomistic molecular dynamics simulations. We use an ionic model to mimic mica surface charge density but without a long-range electric field above the surface, a silica model with a long-range electric field similar to that found experimentally, and an Au {111} model with no partial charges or electric field. A detailed description of the adsorption processes and the contrasts between the various model surfaces is provided. In the case of our model silica surface with a long-range electrostatic field, the adsorption is rapid and primarily driven by electrostatics. Because it is negatively charged (?1e), FN III9 readily adsorbs to a positively charged surface. However, due to its partial charge distribution, FNIII9 can also adsorb to the negatively charged mica model because of the absence of a long-range repulsive electric field. The protein dipole moment dictates its contrasting orientation at these surfaces, and the anchoring residues have opposite charges to the surface. Adsorption on the model Au {111} surface is possible, but less specific, and various protein regions might be involved in the interactions with the surface. Despite strongly influencing the protein mobility, adsorption at these model surfaces does not require wholesale FNIII9 conformational changes, which suggests that the biological activity of the adsorbed protein might be preserved.