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Effect of Nanoparticle Morphology on Protein Adsorbtion

NSF Nanoscale Science and Engineering Center for Directed Assembly of Nanostructures Rensselaer Polytechnic Institute, DMR 0642573. Effect of Nanoparticle Morphology on Protein Adsorbtion. Richard Siegel, Rensselaer Polytechnic Institute, DMR 0642573.

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Effect of Nanoparticle Morphology on Protein Adsorbtion

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  1. NSF Nanoscale Science and Engineering Center for Directed Assembly of Nanostructures Rensselaer Polytechnic Institute, DMR 0642573 Effect of Nanoparticle Morphology on Protein Adsorbtion Richard Siegel, Rensselaer Polytechnic Institute, DMR 0642573 (A) Gold nanospheres (AuNS) and (B) gold nanorods (AuNR) have been synthesized in high yield, and a-chymotrypsin (ChT) and (Lyz) have been adsorbed on the nanoparticle surface. Adsorbtion proceeds in three regions as pictured in (C); in Region I, protein binds to the surface but is not structurally perturbed. In the transition Region II, protein-surface interactions cause the protein to shift conformation. In Region III, protein-protein interactions dominate. ChT-AuNS conjugates only progress to Region I, while ChT-AuNR reach Region III with multilayers forming on the cylindrical cylindrical surface of the AuNR. Lyz-AuNS and AuNR reach Region II, where protein-surface interactions cause aggregation of the conjugates. Future work will focus on the effect of negative curvature and crowding on adsorbed proteins using (D) hollowed gold nanocages with pores varied from 5nm-30nm; protein structure inside the cage (E) will be observed.

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