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Title: SANS study of interaction of silica nanoparticles with BSA protein and their resultant structure

Small angle neutron scattering (SANS) has been carried out to study the interaction of anionic silica nanoparticles (88 Å) with globular protein Bovine Serum Albumin (BSA) (M.W. 66.4 kD) in aqueous solution. The measurements have been carried out on fixed concentration (1 wt %) of Ludox silica nanoparticles with varying concentration of BSA (0–5 wt %) at pH7. Results show that silica nanoparticles and BSA coexist as individual entities at low concentration of BSA where electrostatic repulsive interactions between them prevent their aggregation. However, as the concentration of BSA increases (≥ 0.5 wt %), it induces the attractive depletion interaction among nanoparticles leading to finally their aggregation at higher BSA concentration (2 wt %). The aggregates are found to be governed by the diffusion limited aggregation (DLA) morphology of fractal nature having fractal dimension about 2.4.
Authors:
;  [1] ;  [2]
  1. Solid State Physics Division, Bhabha Atomic Research Centre, Mumbai-400085 (India)
  2. Laboratory for Neutron Scattering, Paul Scherrer Institute, CH-5232 PSI Villigen Switzerland (Switzerland)
Publication Date:
OSTI Identifier:
22269425
Resource Type:
Journal Article
Resource Relation:
Journal Name: AIP Conference Proceedings; Journal Volume: 1591; Journal Issue: 1; Conference: 58. DAE solid state physics symposium 2013, Patiala, Punjab (India), 17-21 Dec 2013; Other Information: (c) 2014 AIP Publishing LLC; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY; 77 NANOSCIENCE AND NANOTECHNOLOGY; 60 APPLIED LIFE SCIENCES; ABUNDANCE; AGGLOMERATION; ALBUMINS; AQUEOUS SOLUTIONS; CATTLE; INTERACTIONS; NANOSTRUCTURES; NEUTRON DIFFRACTION; PARTICLES; SILICA; SMALL ANGLE SCATTERING