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Title: Tuning structure of oppositely charged nanoparticle and protein complexes

Small-angle neutron scattering (SANS) has been used to probe the structures of anionic silica nanoparticles (LS30) and cationic lyszyme protein (M.W. 14.7kD, I.P. ∼ 11.4) by tuning their interaction through the pH variation. The protein adsorption on nanoparticles is found to be increasing with pH and determined by the electrostatic attraction between two components as well as repulsion between protein molecules. We show the strong electrostatic attraction between nanoparticles and protein molecules leads to protein-mediated aggregation of nanoparticles which are characterized by fractal structures. At pH 5, the protein adsorption gives rise to nanoparticle aggregation having surface fractal morphology with close packing of nanoparticles. The surface fractals transform to open structures of mass fractal morphology at higher pH (7 and 9) on approaching isoelectric point (I.P.)
Authors:
;  [1] ;  [2]
  1. Solid State Physics Division, Bhabha Atomic Research Centre, Mumbai-400085 (India)
  2. Institut Laue Langevin, DS/LSS, 6 rue Jules Horowitz, 38042 Grenoble Cedex 9 (France)
Publication Date:
OSTI Identifier:
22269381
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:
71 CLASSICAL AND QUANTUM MECHANICS, GENERAL PHYSICS; 77 NANOSCIENCE AND NANOTECHNOLOGY; ADSORPTION; AGGLOMERATION; FRACTALS; INTERACTIONS; NANOSTRUCTURES; NEUTRON DIFFRACTION; PARTICLES; PROTEINS; SILICA; SMALL ANGLE SCATTERING; SURFACES