TY - JOUR
T1 - Supraparticle Nanoassemblies with Enzymes
AU - Silveira, Gleiciani De Q.
AU - Ramesar, Naomi S.
AU - Nguyen, Trung Dac
AU - Bahng, Joong Hwan
AU - Glotzer, Sharon C.
AU - Kotov, Nicholas A.
N1 - Funding Information:
The work is supported by the US Department of Defense under grant awards no. MURI W911NF-12-1-0407, and by the U.S. Army Research Office under Grant Award No. W911NF- 10-1-0518 (S.C.G). The work of G.d.Q.S., N.S.R., and N.A.K. was funded by Materials Research and Engineering Center, CPHOM, funded by NSF under DMR1120923. N.A.K. also wishes to acknowledge support from NSF under grant ECS-0601345; CBET 0933384; CBET 0932823; and CBET 1036672. T.D.N. was supported by the Vietnam National Foundation for Science and Technology Development (NAFOSTED) under grant no. 103.01-2015.52. We thank the University of Michigan Center for Materials Characterization (MC)2 for use of electron microscopy, and NSF grants (numbers DMR-0320740 and DMR-9871177) for funding the FEI Nova Nanolab Dualbeam Focused Ion Beam Workstation and scanning electron microscope and the JEM-2010F analytical electron microscope used in this work.
Funding Information:
The work is supported by the US Department of Defense under grant awards no. MURI W911NF-12-1-0407, and by the U.S. Army Research Office under Grant Award No. W911NF-10-1-0518 (S.C.G). The work of G.d.Q.S., N.S.R., and N.A.K. was funded by Materials Research and Engineering Center, CPHOM, funded by NSF under DMR1120923. N.A.K. also wishes to acknowledge support from NSF under grant ECS-0601345; CBET 0933384; CBET 0932823; and CBET 1036672. T.D.N. was supported by the Vietnam National Foundation for Science and Technology Development (NAFOSTED) under grant no. 103.01-2015.52. We thank the University of Michigan Center for Materials Characterization (MC) 2 for use of electron microscopy, and NSF grants (numbers DMR-0320740 and DMR-9871177) for funding the FEI Nova Nanolab Dualbeam Focused Ion Beam Workstation and scanning electron microscope and the JEM-2010F analytical electron microscope used in this work.
Publisher Copyright:
© 2019 American Chemical Society.
PY - 2019/9/24
Y1 - 2019/9/24
N2 - Supraparticles are micelle-like self-limited assemblies from inorganic nanoparticles (NPs), whose size and morphology are determined by the equilibrium between short-range attraction and long-range repulsion forces. They can be spontaneously assembled from a variety of nanoscale components that are, in the majority of cases, the same NPs. Hybrid supraparticles made from inorganic and biological components are possible but hardly known. We report here the self-assembly of hybrid bioinorganic supraparticles, prepared from iron disulfide, cadmium telluride, and zinc oxide NPs as well as protease, cytochrome c, and formate dehydrogenase, in which the protein content can exceed that of NPs by 3:1. The resulting bioinorganic supraparticles are 70-150 nm in diameter and have a narrow size distribution. Five different permutations of inorganic and biological components indicate the generality of the observed phenomena. Coarse-grained molecular dynamics simulations confirmed that the formation of supraparticles depends on the interplay between attraction strengths and electrostatic repulsion. Enzymatic activity of the native protein is retained and is completely recovered from the assemblies, which suggests that the supraparticles can be utilized for encapsulation of biomolecules.
AB - Supraparticles are micelle-like self-limited assemblies from inorganic nanoparticles (NPs), whose size and morphology are determined by the equilibrium between short-range attraction and long-range repulsion forces. They can be spontaneously assembled from a variety of nanoscale components that are, in the majority of cases, the same NPs. Hybrid supraparticles made from inorganic and biological components are possible but hardly known. We report here the self-assembly of hybrid bioinorganic supraparticles, prepared from iron disulfide, cadmium telluride, and zinc oxide NPs as well as protease, cytochrome c, and formate dehydrogenase, in which the protein content can exceed that of NPs by 3:1. The resulting bioinorganic supraparticles are 70-150 nm in diameter and have a narrow size distribution. Five different permutations of inorganic and biological components indicate the generality of the observed phenomena. Coarse-grained molecular dynamics simulations confirmed that the formation of supraparticles depends on the interplay between attraction strengths and electrostatic repulsion. Enzymatic activity of the native protein is retained and is completely recovered from the assemblies, which suggests that the supraparticles can be utilized for encapsulation of biomolecules.
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U2 - 10.1021/acs.chemmater.9b02216
DO - 10.1021/acs.chemmater.9b02216
M3 - Article
AN - SCOPUS:85072632623
VL - 31
SP - 7493
EP - 7500
JO - Chemistry of Materials
JF - Chemistry of Materials
SN - 0897-4756
IS - 18
ER -