| Autor: |
Kihara S; School of Chemical Sciences , The University of Auckland , Auckland 1010 , New Zealand.; The MacDiarmid Institute for Advanced Materials and Nanotechnology , Wellington 6140 , New Zealand., van der Heijden NJ; School of Chemical Sciences , The University of Auckland , Auckland 1010 , New Zealand.; The MacDiarmid Institute for Advanced Materials and Nanotechnology , Wellington 6140 , New Zealand., Seal CK; School of Chemical Sciences , The University of Auckland , Auckland 1010 , New Zealand.; The MacDiarmid Institute for Advanced Materials and Nanotechnology , Wellington 6140 , New Zealand., Mata JP; Australian Centre for Neutron Scattering , Australian Nuclear Science and Technology Organisation , Lucas Heights , New South Wales 2234 , Australia., Whitten AE; Australian Centre for Neutron Scattering , Australian Nuclear Science and Technology Organisation , Lucas Heights , New South Wales 2234 , Australia., Köper I; Institute for Nanoscale Science and Technology, College for Science and Engineering , Flinders University , Adelaide , South Australia 5042 , Australia., McGillivray DJ; School of Chemical Sciences , The University of Auckland , Auckland 1010 , New Zealand.; The MacDiarmid Institute for Advanced Materials and Nanotechnology , Wellington 6140 , New Zealand. |
| Abstrakt: |
Upon contact with biological fluids, the surface of nanoparticles is surrounded by many types of proteins, forming a so-called "protein corona". The physicochemical properties of the nanoparticle/corona complex depend predominantly on the nature of the protein corona. An understanding of the structure of the corona and the resulting complex provides insight into the structure-activity relationship. Here, we structurally evaluate the soft and hard components of the protein corona, formed from polystyrene (PS) nanoplastics and human serum albumin (HSA). Using circular dichroism spectroscopy to elucidate the structure of HSA within the complex, we establish the effect of nanoparticle size and pH on the nature of the protein corona formed- whether hard or soft. Despite the weak interaction between PS and the HSA corona, small angle neutron scattering revealed the formation of a complex structure that enhanced the intermolecular interactions between HSA proteins, PS particles, and the HS/PSA complexes. Fractal formation occurred under conditions where the interaction between PS and HSA was strong, and increasing HSA concentrations suppressed the degree of aggregation. The size of the nanoparticles directly influenced the nature of the protein corona, with larger particles favoring the formation of a soft corona, due to the decreased PS-HSA attraction. |
