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. 2013 Dec 7;3(12):986–1003. doi: 10.7150/thno.4827

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© Ivyspring International Publisher. This is an open-access article distributed under the terms of the Creative Commons License (http://creativecommons.org/licenses/by-nc-nd/3.0/). Reproduction is permitted for personal, noncommercial use, provided that the article is in whole, unmodified, and properly cited.

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(a) The CLIO NPs (shown as red spheres) have been modified with either Thrm-A, A DNA aptamer (shown as blue lines) that binds to fibrinogen-recognition exosite of thrombin, or Thrm-B, a DNA aptamer (shown as green lines) that binds to the heparin-binding exosite of thrombin. Addition of thrombin consisting of both fibrinogen (as blue donut) and heparin (as green donuts) exosites resulted in aggregation of CLIO NP assembly, reducing the T2 relaxation time. The DNA sequences are shown at the bottom. The drawing is not to scale. (b) Contrast change in T2-weighted MR image in 1:1 CLIO-Thrm-A and CLIO-Thrm-B mixture with 0, 10, 25 and 50 nM thrombin (first column), BSA (second column) and streptavidin (third column). Reproduced with permission from Ref. 36. Copyright (2008) American Chemical Society.