Conformational flexibility of fatty acid-free bovine serum albumin proteins enables superior antifouling coatings
Open Access
- 17 July 2020
- journal article
- research article
- Published by Springer Nature in Communications Materials
- Vol. 1 (1) , 1-11
Abstract
Bovine serum albumin (BSA) protein is widely used to fabricate antifouling coatings for nanobiotechnology applications. Numerous BSA protein options are commercially available and obtained through different purification methods, however, there is no guidance on which ones are preferable for antifouling coatings. Herein, we investigate the real-time fabrication of antifouling coatings composed of BSA proteins obtained through different purification methods, and report significant differences in ultrathin film coating properties and ability to mitigate serum biofouling and to prevent nanoparticle-induced immune reactions. Mechanistic studies unravel the source of these performance variations, which are related to some BSA proteins containing fatty acid stabilizers while other BSA proteins are fatty acid-free depending on the purification method. Fatty acid-free BSA proteins exhibit greater conformational flexibility and less charge repulsion, which allow them to form more rigidly attached and tightly packed coatings on flat surfaces and nanoparticles that result in superior application performance.Keywords
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Funding Information
- National Research Foundation Singapore (NRF2015NRF-POC0001-19)
This publication has 58 references indexed in Scilit:
- Fiji: an open-source platform for biological-image analysisNature Methods, 2012
- Antibiotic susceptibility patterns of urinary pathogens in female outpatientsNorth American Journal of Medical Sciences, 2012
- Understanding protein adsorption phenomena at solid surfacesAdvances in Colloid and Interface Science, 2011
- Complement: a key system for immune surveillance and homeostasisNature Immunology, 2010
- Efficiency of blocking of non-specific interaction of different proteins by BSA adsorbed on hydrophobic and hydrophilic surfacesJournal of Colloid and Interface Science, 2010
- Infrared spectroscopy of proteinsBiochimica et Biophysica Acta (BBA) - Bioenergetics, 2007
- Surface Tailoring for Controlled Protein Adsorption: Effect of Topography at the Nanometer Scale and ChemistryJournal of the American Chemical Society, 2006
- Reduction of Irreversible Protein Adsorption on Solid Surfaces by ProteinEngineering for IncreasedStabilityJournal of Biological Chemistry, 2005
- Interaction of an apolipoprotein (apoLP-alanine) with phosphatidylcholineBiochemistry, 1973
- Preparation and Properties of Serum and Plasma Proteins. IV. A System for the Separation into Fractions of the Protein and Lipoprotein Components of Biological Tissues and Fluids1a,b,c,dJournal of the American Chemical Society, 1946