Download
1 / 1
10 likes | 153 Views
Schematic showing possible arrangement of fibrinogen molecules on a protruding 11- nm cationic nanoparticle . Seed 1. Capturing Clustering Proteins on Surface-Immobilized Nanoparticles.
E N D
Schematic showing possible arrangement of fibrinogen molecules on a protruding 11- nm cationic nanoparticle. Seed 1. Capturing Clustering Proteins on Surface-Immobilized Nanoparticles A collaboration between the Santore and Rotello labs has produced surfaces with isolated immobilized functionalized gold nanoparticles. Relatively short hydrated polymer brushes, backfilled on the surface around the nanoparticles, allow protrusion of the nanoparticles which then adsorb protein. 11-nm diameter nanoparticles, in this case with cationic functionality, protrude from the brush and adsorb protein in a highly clustered fashion. Reflectometry measurements indicate more than 50 proteins per nanoparticle, a surprising result for fibrinogen adsorption because of its 47-nm length. Fibrinogen’s small 4.5 nm diameter, giving a high aspect ratio, along with the sharp nanoparticle curvature is thought to facilitate this high protein loading. On a mass per area basis, this amounts to about 170 mg/m2, compared with 5 mg/m2 on flat surfaces of similar functionality. This important result may facilitate the creation of highly sensitive detection elements, but also has strong implications for how nanoparticles interact with blood and in the environment. (M. Santore, V. Rotello, J. Zhang, B. Fang, S. Gon, R. Gettens, J. Criscuolo, S. Kalasin) DMR-0820506
