Nanoplastics – protein interaction: a scattering study of transition from soft and hard corona

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dc.contributor.authorKihara, Sen_AU
dc.contributor.authorKoeper, Ien_AU
dc.contributor.authorSeal, Cen_AU
dc.contributor.authorMcGillivray, DJen_AU
dc.contributor.authorMata, JPen_AU
dc.date.accessioned2023-11-22T21:45:18Zen_AU
dc.date.available2023-11-22T21:45:18Zen_AU
dc.date.issued2018-11-19en_AU
dc.date.statistics2023-07-05en_AU
dc.description.abstractThere is growing concern about plastic waste in the environment, and its impact on biological organisms. While bulk plastics are thought to be non-toxic, when the plastics break down to a sub-micron length scale (i.e. nanoplastics), they obtain extra mobility inside living things, and may cause various adverse effects [1,2]. This, coupled with a lack of knowledge surrounding the dangers from different types of plastics, prevents well-designed responses to the problem. Hypothetically, the potential adverse effects are caused by protein denaturation, oxidative stress and/or cellular mem brane damage. However, the inherent complexity of biological systems makes it challenging to gain a mechanistic understanding. Adding complexity to this problem, the potential adverse effects are highly dependent on the nature of nanoparticles (NPs) – the contributing factors could include elemental composition, chemistry of the plastic surface, and/or size of the plastic particle [3,2,4]. When in biological systems, nanoplastics are surrounded by various types of proteins5. The structure of proteins surrounding nanoplastics are important parameters to understand the interaction of nanoplastic/protein composite. We carried out light scattering and small angle neutron scattering (SANS) experiments to explore the structure of the protein corona on monodisperse polystyrene spheres using a model protein human serum albumin (HSA). The geometry of the PS/HSA complex was investigated with a contrast matching method. The transition from a “soft” to a “hard” interaction between the nanoparticle and the protein was observed when pH is lowered from 7.4, and the implications of this on nanoplastic toxicity is discussed. © The Authors.en_AU
dc.identifier.citationKihara, S., Koeper, I., Seal, C., McGillivray, D., & Mata, J. (2018). Nanoplastics – protein interaction: a scattering study of transition from soft and hard corona. Presetation to ANBUG-AINSE Neutron Scattering Symposium, AANSS 2018, 19 - 21 November 2018, Sydney, Australia, (pp. 21). Retrieved from https://events01.synchrotron.org.au/event/84/book-of-abstracts.pdfen_AU
dc.identifier.conferenceenddate2018-11-21en_AU
dc.identifier.conferencenameANBUG-AINSE Neutron Scattering Symposium, AANSS 2018en_AU
dc.identifier.conferenceplaceLucas Heights, New South Walesen_AU
dc.identifier.conferencestartdate2018-11-19en_AU
dc.identifier.pagination21en_AU
dc.identifier.urihttps://apo.ansto.gov.au/handle/10238/15234en_AU
dc.language.isoenen_AU
dc.publisherAustralian Institute of Nuclear Science and Engineering (AINSE)en_AU
dc.relation.urihttps://events01.synchrotron.org.au/event/84/book-of-abstracts.pdfen_AU
dc.subjectPlasticsen_AU
dc.subjectWastesen_AU
dc.subjectEnvironmenten_AU
dc.subjectNanoparticlesen_AU
dc.subjectProteinsen_AU
dc.subjectScatteringen_AU
dc.subjectSmall angle scatteringen_AU
dc.titleNanoplastics – protein interaction: a scattering study of transition from soft and hard coronaen_AU
dc.typeConference Abstracten_AU
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