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A Metal Organic Framework with Spherical Protein Nodes: Rational Chemical Design of 3D Protein Crystals
Author(s) -
Pamela A. Sontz,
J.B. Bailey,
Sunhyung Ahn,
F.A. Tezcan
Publication year - 2015
Publication title -
journal of the american chemical society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.115
H-Index - 612
eISSN - 1520-5126
pISSN - 0002-7863
DOI - 10.1021/jacs.5b07463
Subject(s) - chemistry , linker , crystallography , ferritin , ternary operation , metal , rational design , octahedron , metal organic framework , protein crystallization , crystal structure , stereochemistry , crystallization , nanotechnology , organic chemistry , biochemistry , materials science , adsorption , computer science , programming language , operating system
We describe here the construction of a three-dimensional, porous, crystalline framework formed by spherical protein nodes that assemble into a prescribed lattice arrangement through metal-organic linker-directed interactions. The octahedral iron storage enzyme, ferritin, was engineered in its C3 symmetric pores with tripodal Zn coordination sites. Dynamic light scattering and crystallographic studies established that this Zn-ferritin construct could robustly self-assemble into the desired bcc-type crystals upon coordination of a ditopic linker bearing hydroxamic acid functional groups. This system represents the first example of a ternary protein-metal-organic crystalline framework whose formation is fully dependent on each of its three components.

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