How negatively charged proteins adsorb to negatively charged surfaces - a molecular dynamics study of BSA adsorption on silica
Kubiak-Ossowska, Karina and Jachimska, Barbara and Mulheran, Paul A. (2016) How negatively charged proteins adsorb to negatively charged surfaces - a molecular dynamics study of BSA adsorption on silica. Journal of Physical Chemistry B, 120 (40). pp. 10463-10468. ISSN 1520-6106 (https://doi.org/10.1021/acs.jpcb.6b07646)
Preview |
Text.
Filename: Kubiak_Ossowska_etal_JPCB_2016_How_negatively_charged_proteins_adsorb_to_negatively_charged_surfaces.pdf
Accepted Author Manuscript Download (1MB)| Preview |
Abstract
How proteins adsorb to inorganic material surfaces is critically important for the development of new biotechnologies, since the orientation and structure of the adsorbed proteins impacts their functionality. Whilst it is known that many negatively charged proteins readily adsorb to negatively charged oxide surfaces, a detailed understanding of how this process occurs is lacking. In this work we study the adsorption of BSA, an important transport protein that is negatively charged at physiological conditions, to a model silica surface that is also negatively charged. We use fully atomistic Molecular Dynamics to provide detailed understanding of the non-covalent interactions that bind the BSA to the silica surface. Our results provide new insight into the competing roles of long-range electrostatics and short-range forces, and the consequences this has for the orientation and structure of the adsorbed proteins.
ORCID iDs
Kubiak-Ossowska, Karina, Jachimska, Barbara and Mulheran, Paul A. ORCID: https://orcid.org/0000-0002-9469-8010;-
-
Item type: Article ID code: 58414 Dates: DateEvent13 October 2016Published22 September 2016Published Online22 September 2016AcceptedSubjects: Science > Chemistry Department: Faculty of Engineering > Chemical and Process Engineering Depositing user: Pure Administrator Date deposited: 01 Nov 2016 15:08 Last modified: 26 Oct 2024 00:27 Related URLs: URI: https://strathprints.strath.ac.uk/id/eprint/58414