Protein interactions with negatively charged inorganic surfaces
Kubiak-Ossowska, Karina and Jachimska, Barbara and Al Qaraghuli, Mohammed and Mulheran, Paul A. (2019) Protein interactions with negatively charged inorganic surfaces. Current Opinion in Colloid and Interface Science, 41. pp. 104-117. ISSN 1359-0294 (https://doi.org/10.1016/j.cocis.2019.02.001)
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Abstract
Protein adsorption on charged inorganic solid materials has recently attracted enormous interest owing to its various possible applications, including drug delivery and biomaterial design. The need to combine experimental and computational approaches to get a detailed picture of the adsorbed protein properties is increasingly recognised and emphasised in this review. We discuss the methods frequently used to study protein adsorption and the information they can provide. We focus on model systems containing a silica surface, which is negatively charged and hydrophilic at physiological pH, and two contrasting proteins: bovine serum albumin (BSA) and lysozyme (LSZ) that are both water soluble. At pH 7, BSA has a net negative charge, whereas LSZ is positive. In addition, BSA is moderately sized and flexible, whereas LSZ is small and relatively rigid. These differences in charge and structural nature capture the role of electrostatics and hydrophobic interactions on the adsorption of these proteins, along with the impact of adsorption on protein orientation and function. Understanding these model systems will undoubtedly enhance the potential to extrapolate our knowledge to other systems of interest.
ORCID iDs
Kubiak-Ossowska, Karina, Jachimska, Barbara, Al Qaraghuli, Mohammed ORCID: https://orcid.org/0000-0003-1823-6671 and Mulheran, Paul A. ORCID: https://orcid.org/0000-0002-9469-8010;-
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Item type: Article ID code: 67406 Dates: DateEvent1 June 2019Published8 February 2019Published Online1 February 2019AcceptedSubjects: Technology > Chemical engineering Department: Faculty of Science > Physics
Faculty of Engineering > Chemical and Process EngineeringDepositing user: Pure Administrator Date deposited: 21 Mar 2019 16:14 Last modified: 03 Dec 2024 21:55 Related URLs: URI: https://strathprints.strath.ac.uk/id/eprint/67406