Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/151369
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dc.contributor.authorPark, Jae Hyeonen_US
dc.contributor.authorFerhan, Abdul Rahimen_US
dc.contributor.authorJackman, Joshua A.en_US
dc.contributor.authorCho, Nam-Joonen_US
dc.date.accessioned2021-07-09T02:17:21Z-
dc.date.available2021-07-09T02:17:21Z-
dc.date.issued2019-
dc.identifier.citationPark, J. H., Ferhan, A. R., Jackman, J. A. & Cho, N. (2019). Modulating conformational stability of human serum albumin and implications for surface passivation applications. Colloids and Surfaces B: Biointerfaces, 180, 306-312. https://dx.doi.org/10.1016/j.colsurfb.2019.04.017en_US
dc.identifier.issn0927-7765en_US
dc.identifier.other0000-0002-2266-943X-
dc.identifier.other0000-0002-8692-8955-
dc.identifier.urihttps://hdl.handle.net/10356/151369-
dc.description.abstractHuman serum albumin (HSA) is one of the most abundant proteins in the human body and also used as a biomaterial coating. While there is significant interest in modifying the properties of solid supports to control HSA adsorption, there is an outstanding need to investigate whether modulating the conformational properties of HSA proteins can influence adsorption properties, especially in the context of surface passivation applications. Herein, we investigated how ionic strength – a key modulator of electrostatic forces influencing protein folding and protein-substrate interactions – can affect the conformational stability of HSA proteins and the resulting adsorption of HSA proteins onto silica surfaces for surface passivation applications. Thermal denaturation experiments identified that HSA is prone to unfolding and aggregation under physiologically relevant ionic strength conditions while HSA is more conformationally stable in low salt conditions. In line with these observations, we also determined that the adsorption of native HSA monomers onto silica surfaces was strongly influenced by electrostatic forces, with greater uptake in low ionic strength conditions. By contrast, the adsorption uptake of heat-denatured HSA was greatest in high ionic strength conditions and related to oligomer size. It was further revealed that native HSA is superior to heat-denatured HSA for passivating silica surfaces against serum biofouling. Taken together, our findings demonstrate that modulating the conformational stability of HSA proteins influences the adsorption pathway and passivation properties, offering fundamental insights that can lead to improved protein coatings.en_US
dc.description.sponsorshipNanyang Technological Universityen_US
dc.description.sponsorshipNational Research Foundation (NRF)en_US
dc.language.isoenen_US
dc.relationNRFCRP10-2012-07en_US
dc.relationNRF2015NRFPOC0001-19en_US
dc.relation.ispartofColloids and Surfaces B: Biointerfacesen_US
dc.rights© 2019 Elsevier B.V. All rights reserved.en_US
dc.subjectEngineering::Materialsen_US
dc.titleModulating conformational stability of human serum albumin and implications for surface passivation applicationsen_US
dc.typeJournal Articleen
dc.contributor.schoolSchool of Materials Science and Engineeringen_US
dc.contributor.schoolSchool of Chemical and Biomedical Engineeringen_US
dc.identifier.doi10.1016/j.colsurfb.2019.04.017-
dc.identifier.pmid31071570-
dc.identifier.scopus2-s2.0-85065056637-
dc.identifier.volume180en_US
dc.identifier.spage306en_US
dc.identifier.epage312en_US
dc.subject.keywordsProtein Adsorptionen_US
dc.subject.keywordsProtein Aggregationen_US
dc.description.acknowledgementThis work was supported by the National Research Foundation of Singapore through a Competitive Research Programme grant (NRFCRP10-2012-07) and a Proof-of-Concept grant (NRF2015NRFPOC0001-19) as well as through the Center for Precision Biology at Nanyang Technological University. Additional support was provided by the Creative Materials Discovery Program through the National Research Foundation of Korea funded by the Ministry of Science, ICT and Future Planning (NRF-2016M3D1A1024098).en_US
item.grantfulltextnone-
item.fulltextNo Fulltext-
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