Identifying specific protein residues that guide surface interactions and orientation on silica nanoparticles

Siddhartha Shrivastava, Scott A. McCallum, Joseph H. Nuffer, Xi Qian, Richard W. Siegel, Jonathan S. Dordick

Research output: Contribution to journalArticlepeer-review

23 Scopus citations

Abstract

We identify specific acylphosphatase (AcP) residues that interact with silica nanoparticles (SNPs) using a combined NMR spectroscopy and proteomics-mass spectrometry approach. AcP associated with 4- and 15-nm diameter SNPs through a common and specific interaction surface formed by amino acids from the two α-helices of the protein. Greater retention of native protein structure was obtained on 4-nm SNPs than on 15-nm particles, presumably due to greater surface curvature-induced protein stabilization with the smaller SNPs. These results demonstrate that proteins may undergo specific and size-dependent orientation on nanoparticle surfaces. Our approach can be broadly applied to various protein-material systems to help understand in much greater detail the protein-nanomaterial interface; it would also encourage better modeling, and thus prediction and design, of the behavior of functional proteins adsorbed onto different surfaces.

Original languageEnglish (US)
Pages (from-to)10841-10849
Number of pages9
JournalLangmuir
Volume29
Issue number34
DOIs
StatePublished - Aug 27 2013

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