A Library of Protein Cage Architectures as Nanomaterials
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- A Library of Protein Cage Architectures as Nanomaterials
- Flenniken, M. L.; Uchida, M.; Liepold, L. O.; Kang, Sebyung; Young, M. J.; Douglas, T.
- COWPEA MOSAIC-VIRUS; MRI CONTRAST AGENTS; HEAT-SHOCK-PROTEIN; CHLOROTIC MOTTLE VIRUS; SUPRAMOLECULAR BUILDING-BLOCKS; DPS-LIKE PROTEIN; PHAGE DISPLAY; IN-VIVO; METHANOCOCCUS-JANNASCHII; VIRAL NANOPARTICLES
- Issue Date
- SPRINGER-VERLAG BERLIN
- CURRENT TOPICS IN MICROBIOLOGY AND IMMUNOLOGY, v.327, no., pp.71 - 93
- Virus capsids and other structurally related cage-like proteins such as ferritins, dps, and heat shock proteins have three distinct surfaces (inside, outside, interface) that can be exploited to generate nanomaterials with multiple functionality by design. Protein cages are biological in origin and each cage exhibits extremely homogeneous size distribution. This homogeneity can be used to attain a high degree of homogeneity of the templated material and its associated property. A series of protein cages exhibiting diversity in size, functionality, and chemical and thermal stabilities can be utilized for materials synthesis under a variety of conditions. Since synthetic approaches to materials science often use harsh temperature and pH, it is an advantage to utilize protein cages from extreme environments. In this chapter, we review recent studies on discovering novel protein cages from harsh natural environments such as the acidic thermal hot springs at Yellowstone National Park (YNP) and on utilizing protein cages as nano-scale platforms for developing nanomaterials with wide range of applications from electronics to biomedicine.
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