TY - GEN
T1 - Protein cage assisted metal-protein nanocomposite synthesis
T2 - International Conference on Nanotechnology - Research and Commercialization 2011, ICONT 2011
AU - Sana, Barindra
AU - Calista, Marcia
AU - Lim, Sierin
PY - 2012
Y1 - 2012
N2 - Ferritin is an iron-storage protein in most living systems with a cage-like structure. It has inherent property to form metallic nanocore within its cavity. The metallic core formed within the Archaeoglobus fulgidus ferritin cavity is stabilized by modulating the protein structure by site directed mutagenesis. Encapsulation protocol of various metals within the engineered ferritin cage (AfFtn-AA) is optimized. Dense metallic cores are visualized using electron microscopy and the bound metal was quantified by ICP-spectrometry. The AfFtn-AA is loaded with up to about 350 cobalt, 2000 chromium, and as high as 7000 iron atoms, separately. The metal-protein nanocomposites formed by encapsulation of cobalt, chromium, and iron are studied. Magnetic resonance imaging of the agarose embedded nanocomposites shows brightening of T 1-weighted images and signal loss of T2-weighted images with increasing concentration of the nanocomposites. Shortening of magnetic relaxation times in the presence of the nanocomposites confirm their ability to enhance magnetic relaxation rate and suggests that the nanocomposites have potential application as MRI contrast agent.
AB - Ferritin is an iron-storage protein in most living systems with a cage-like structure. It has inherent property to form metallic nanocore within its cavity. The metallic core formed within the Archaeoglobus fulgidus ferritin cavity is stabilized by modulating the protein structure by site directed mutagenesis. Encapsulation protocol of various metals within the engineered ferritin cage (AfFtn-AA) is optimized. Dense metallic cores are visualized using electron microscopy and the bound metal was quantified by ICP-spectrometry. The AfFtn-AA is loaded with up to about 350 cobalt, 2000 chromium, and as high as 7000 iron atoms, separately. The metal-protein nanocomposites formed by encapsulation of cobalt, chromium, and iron are studied. Magnetic resonance imaging of the agarose embedded nanocomposites shows brightening of T 1-weighted images and signal loss of T2-weighted images with increasing concentration of the nanocomposites. Shortening of magnetic relaxation times in the presence of the nanocomposites confirm their ability to enhance magnetic relaxation rate and suggests that the nanocomposites have potential application as MRI contrast agent.
KW - Archaeoglobus fulgidus
KW - Contrast agent, Protein cage
KW - Ferritin
KW - MRI
UR - http://www.scopus.com/inward/record.url?scp=84874468450&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84874468450&partnerID=8YFLogxK
U2 - 10.1063/1.4769136
DO - 10.1063/1.4769136
M3 - Conference contribution
AN - SCOPUS:84874468450
SN - 9780735411197
T3 - AIP Conference Proceedings
SP - 82
EP - 96
BT - International Conference on Nanotechnology - Research and Commercialization 2011, ICONT 2011
Y2 - 6 June 2011 through 9 June 2011
ER -