Protein-Polymer Functionalized Aqueous Ferrofluids Showing High T2 Relaxivity

Bhattacharya, S and Sheikh, Lubna and Tiwari, V and Ghosh, M and Patel, J N and Patel, A B and Nayar, S (2014) Protein-Polymer Functionalized Aqueous Ferrofluids Showing High T2 Relaxivity. Journal of Biomedical Nanotechnology, 10(5) (IF-7.578). pp. 811-819.

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Controlled size, shape and dispersibility of superparamagnetic iron oxide nanoparticles (SPIONs), has been achieved in a protein-polymer colloidal dispersion. Stable ferrofluid (FF) is synthesized in an aqueous medium of collagen, bovine serum albumin and poly(vinyl) alcohol that equilibrates with time, at ambient conditions, into an organized matrix with iron oxide particles sterically caged at defined sites. It mimics a biomineralization system; hence the process is termed biomimetics. Though the exact mechanism is not understood at this stage, we have established, with serial dilution of the protein-polymer solution that the SPIONs are formed inside the self-contained clusters of the two proteins and the polymer, which show a tendency to self assemble. More than the interparticle dipolar attractions of magnetic particles, electrostatic interactions play a role in cluster formation and collagen is responsible for the overall stability, supported by systematic dynamic light scattering data. The basic aim of this study was to increase magnetization of a previously synthesized ferrofluid without hampering stability, reducing the total macromolecular concentration. Thrice the magnetization was achieved and in addition, the synthesized FFs exhibited very high transverse relaxivity and showed good contrast in mice liver, in the in vivo studies

Item Type:Article
Official URL/DOI:
Uncontrolled Keywords:Aqueous FFs; Biomimetics; Biomineralization; Self-Assembly; T2 Relaxivity
Divisions:Metal Extraction and Forming
ID Code:6820
Deposited By:Sahu A K
Deposited On:23 Jan 2014 17:48
Last Modified:04 May 2016 12:43
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