Self-Assembly of Protein Cage Directed Nanoparticle Superlattices. Mauri Kostiainen Aalto University Department of Applied Physics
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1 Self-Assembly of Protein Cage Directed Nanoparticle Superlattices Mauri Kostiainen Aalto University Department of Applied Physics
2 Protein Nanoparticles Protein cages (e.g viruses) as building blocks for nanomaterials Consist of a discrete number of protein subunits Well-defined size and shape Reversible assembly Hollow interior Encapsulation of nanoparticles inside protein cages induce assembly The protein cage can in principle controll the assembly of any material that is encapsulated inside it rdered 3D arrays of protein cages with material inside
3 Protein Cage Details RNA Cowpea chlorotic mottle virus (CCMV) Capsid diameter 28 nm Cavity diameter 18 nm Native virus particle (RNA genome inside) pi 3.7 FT cage with: 1. Hollow cavity (apoft) 2. -Fe 2 3 (MF) Ferritin from Pyrococcus furiosus Cage diameter 12 nm Cavity diameter 8 nm Magnetoferritin (6 nm Fe 3 4 -Fe 2 3 particles inside) Superparamagnetic pi 4.5
4 CCMV Purification Californian black-eye beans - Two weeks of gardening - Four kilos of plant material - Two days of purification Plants growing Homogenized plant 1 g of pure CCMV Final CsCl density gradient ultracentrifugation Native CCMV virus particles SEC-trace of purified CCMV
5 Negatively Charged Cages induce assembly Electrostatic approach to assemble ordered protein cage arrays? Assembly of protein cages Both cages are negatively charged at neutral ph. The negatively charged patches on CCMV are located around the three-fold rotation axes Interaction with Cationic nanoparticles CCMV Electrostatic potential projected on the solvent accessible surface: red -9 kt/e and blue 0 kt/e
6 Nanoparticle superlattice Binary nanoparticle superlattice + Au Integrate for example magnetic and plamsonic nanoparticles into one system Au S N +
7 region 1 region 2 region 3 amorphous crystalline (AB 8 fcc ) free particles Small-angle X-ray scattering m AuNP /m CCMV relative degree of crystallinity (%) = Three regions: 1) High binding affinity amorphous gel 2) Moderate affinity crystalline lattices 3) Low affinity free particles ε 0 εk B T 2N a e 2 I 1 ) (nm)(c NaCl )
8 3D structure by cryogenicelectron tomography [100] [110] [100] [110] a AB 8 fcc Bravais lattice: face-centred-cubic _ Space group: Fm3m (225) a = 40.4 nm, d CCMV-CCMV = 28.6 nm
9 I(q) q 2 [a.u] (111) (200) (311) (511) (440) (442) (640) (533) (733) (664) (931) (400) (331) Small-angle X-ray scattering from solution samples confirms the TEM observations Experimental data Fit (finite f.c.c.) fcc Theory (perfect f.c.c.) fcc q (Å -1 ) AB 8 fcc structure is not isostructural to any known atomic or molecular crystal structure and has never been observed with nano-sized particles before
10 What kind of structures can be formed with apoferritin and magnetoferritin? FT cage with: 1. Hollow cavity (apoft) 2. -Fe 2 3 (MF) + Au Au S N +
11 I(q) I(q) q q 2 2 [a.u] (100) (110) (111) (200) (210) (211) I(q) q 2 2 [a.u] (100) (111) (200) (210) (111) (200) (210) (220) (300) (220) (300) (211) (110) I(q) I(q) q q 2 2 [a.u] I(q) q 2 2 [a.u] Apoferritin -1 (nm) -1 (nm) >3 > >3 1.8 > (Å q (Å apoft -1 ) apoft Experimental data Fit Experimental (finite sc) data Theory Fit (finite (perfect sc) sc) Theory (perfect sc) magnetoferritin (nm) > q (Å -1 ) MF Experimental Experimental data data Fit Fit (finite (finite sc) sc) Theory Theory (perfect (perfect sc) sc) (Å q (Å -1 ) q (Å -1-1 ) Apoferritin and magnetoferritin can be assembled into similar crystals structures
12 TEM images of MF-AuNP superlattices along different rotation axis I(q) q 2 [a.u] (100) (110) (111) (200) (210) (211) (220) (300) 1/T 2 (s -1 ) Applications for magnetoferritin assemblies briefly: Preparation of free standing crystals Conrtrast agents for magnetic resonance imaging a = nm MF + AuNP (superlattice) MF + AuNP (free particles) Magnevist r 2 = 56 (s -1 mm -1 ) weighted MRI T 2 c Fe (mm) r 2 = 41 (s -1 mm -1 ) r 2 = 4.8 (s -1 mm -1 ) q (Å -1 ) c Fe (mm)
13 Conclusions: Protein cages can direct the selfassembly of binary nanoparticle superlattices New crystal lattices can be achieved Assemblies are responsive to ph and ionic strength See also: M. Kostiainen et al. Nature Nanotechnology, 2012, doi: /nnano Acknowledgements: Academy of Finland: PostDoc funding for M.A.K. and Programmable Materials project funding (together with P. Törmä,. Ikkala, S. Van Dijken, P. Liljeroth) Emil Aaltonen Foundation, Aalto Starting Grand Co-workers: P. Hiekkataipale, A. Laiho, V. Lemieux, J. Seitsonen, J. Ruokolainen, P. Ceci
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