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Controlling Association and Separation of Gold Nanoparticles with Computationally Designed Zinc-Coordinating Proteins

Title
Controlling Association and Separation of Gold Nanoparticles with Computationally Designed Zinc-Coordinating Proteins
Authors
Eibling M.J.Macdermaid C.M.Qian Z.Lanci C.J.Park S.-J.Saven J.G.
Ewha Authors
박소정
SCOPUS Author ID
박소정scopus
Issue Date
2017
Journal Title
Journal of the American Chemical Society
ISSN
0002-7863JCR Link
Citation
vol. 139, no. 49, pp. 17811 - 17823
Publisher
American Chemical Society
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
Functionalization of nanoparticles with biopolymers has yielded a wide range of structured and responsive hybrid materials. DNA provides the ability to program length and recognition using complementary oligonucleotide sequences. Nature more often leverages the versatility of proteins, however, where structure, assembly, and recognition are more subtle to engineer. Herein, a protein was computationally designed to present multiple Zn2+ coordination sites and cooperatively self-associate to form an antiparallel helical homodimer. Each subunit was unstructured in the absence of Zn2+ or when the cation was sequestered with a chelating agent. When bound to the surface of gold nanoparticles via cysteine, the protein provided a reversible molecular linkage between particles. Nanoparticle association and changes in interparticle separation were monitored by redshifts in the surface plasmon resonance (SPR) band and by transmission electron microscopy (TEM). Titrations with Zn2+ revealed sigmoidal transitions at submicromolar concentrations. The metal-ion concentration required to trigger association varied with the loading of the proteins on the nanoparticles, the solution ionic strength, and the cation employed. Specifying the number of helical (heptad) repeat units conferred control over protein length and nanoparticle separation. Two different length proteins were designed via extension of the helical structure. TEM and extinction measurements revealed distributions of nanoparticle separations consistent with the expected protein structures. Nanoparticle association, interparticle separation, and SPR properties can be tuned using computationally designed proteins, where protein structure, folding, length, and response to molecular species such as Zn2+ can be engineered. © 2017 American Chemical Society.
DOI
10.1021/jacs.7b04786
Appears in Collections:
자연과학대학 > 화학·나노과학전공 > Journal papers
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