Ordering surfaces on the nanoscale

Implications for protein adsorption

Andrew Hung, Steve Mwenifumbo, Morgan Mager, Jeffrey J. Kuna, Francesco Stellacci, Irene Yarovsky, Molly M. Stevens

Research output: Contribution to journalArticle

111 Citations (Scopus)

Abstract

Monolayer-protected metal nanoparticles (MPMNs) are a newly discovered class of nanoparticles with an ordered, striped domain structure that can be readily manipulated by altering the ratio of the hydrophobic to hydrophilic ligands. This property makes them uniquely suited to systematic studies of the role of nanostructuring on biomolecule adsorption, a phenomenon of paramount importance in biomaterials design. In this work, we examine the interaction of the simple, globular protein cytochrome C (Cyt C) with MPMN surfaces using experimental protein assays and computational molecular dynamics simulations. Experimental assays revealed that adsorption of CytC generally increased with increasing surface polar ligand content, indicative of the dominance of hydrophilic interactions in Cyt C-MPMN binding. Protein-surface adsorption enthalpies calculated fromcomputational simulations employing rigid-backbone coarse-grained Cyt C and MPMN models indicate a monotonic increase in adsorption enthalpy with respect to MPMN surface polarity. These results are in qualitative agreement with experimental results and suggest thatCytCdoes not undergo significant structural disruption upon adsorption to MPMN surfaces. Coarse-grained and atomistic simulations furthermore elucidated the important role of lysine in facilitating Cyt C adsorption to MPMN surfaces. The amphipathic character of the lysine side chain enables it to form close contacts with both polar and nonpolar surface ligands simultaneously, rendering it especially important for interactions with surfaces composed of adjacent nanoscale chemical domains.The importance of these structural characteristics of lysine suggests that proteins may be engineered to specifically interact with nanomaterials by targeted incorporation of unnatural amino acids possessing dual affinity to differing chemical motifs.

Original languageEnglish
Pages (from-to)1438-1450
Number of pages13
JournalJournal of the American Chemical Society
Volume133
Issue number5
DOIs
Publication statusPublished - Feb 9 2011

Fingerprint

Metal Nanoparticles
Metal nanoparticles
Adsorption
Monolayers
Proteins
Cytochromes
Lysine
Ligands
Enthalpy
Assays
Nanostructures
Biocompatible Materials
Biomolecules
Molecular Dynamics Simulation
Protein C
Hydrophobic and Hydrophilic Interactions
Nanostructured materials
Nanoparticles
Molecular dynamics
Biomaterials

ASJC Scopus subject areas

  • Chemistry(all)
  • Catalysis
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

Hung, A., Mwenifumbo, S., Mager, M., Kuna, J. J., Stellacci, F., Yarovsky, I., & Stevens, M. M. (2011). Ordering surfaces on the nanoscale: Implications for protein adsorption. Journal of the American Chemical Society, 133(5), 1438-1450. https://doi.org/10.1021/ja108285u

Ordering surfaces on the nanoscale : Implications for protein adsorption. / Hung, Andrew; Mwenifumbo, Steve; Mager, Morgan; Kuna, Jeffrey J.; Stellacci, Francesco; Yarovsky, Irene; Stevens, Molly M.

In: Journal of the American Chemical Society, Vol. 133, No. 5, 09.02.2011, p. 1438-1450.

Research output: Contribution to journalArticle

Hung, A, Mwenifumbo, S, Mager, M, Kuna, JJ, Stellacci, F, Yarovsky, I & Stevens, MM 2011, 'Ordering surfaces on the nanoscale: Implications for protein adsorption', Journal of the American Chemical Society, vol. 133, no. 5, pp. 1438-1450. https://doi.org/10.1021/ja108285u
Hung A, Mwenifumbo S, Mager M, Kuna JJ, Stellacci F, Yarovsky I et al. Ordering surfaces on the nanoscale: Implications for protein adsorption. Journal of the American Chemical Society. 2011 Feb 9;133(5):1438-1450. https://doi.org/10.1021/ja108285u
Hung, Andrew ; Mwenifumbo, Steve ; Mager, Morgan ; Kuna, Jeffrey J. ; Stellacci, Francesco ; Yarovsky, Irene ; Stevens, Molly M. / Ordering surfaces on the nanoscale : Implications for protein adsorption. In: Journal of the American Chemical Society. 2011 ; Vol. 133, No. 5. pp. 1438-1450.
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