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.
Original language | English |
---|---|
Pages (from-to) | 10463-10468 |
Number of pages | 6 |
Journal | Journal of Physical Chemistry B |
Volume | 120 |
Issue number | 40 |
Early online date | 22 Sept 2016 |
DOIs | |
Publication status | Published - 13 Oct 2016 |
Keywords
- proteins
- inorganic materials
Fingerprint
Dive into the research topics of 'How negatively charged proteins adsorb to negatively charged surfaces - a molecular dynamics study of BSA adsorption on silica'. Together they form a unique fingerprint.Profiles
Datasets
-
Bovine Serum Albumin (BSA) Adsorption on Silica
Mulheran, P. (Creator) & Kubiak-Ossowska, K. (Creator), University of Strathclyde, 3 Oct 2016
DOI: 10.15129/40c97bff-5a36-4ed7-a297-e46279930e2a, http://www.archie-west.ac.uk/
Dataset