Nature has evolved dynamic, non-equilibrium mechanisms for assembling hierarchical complexes of nanomaterials. A critical element to
many of these assembly mechanisms involves the active and directed transport of materials by biomolecular motor proteins such as kinesin.
In the present work, nanocrystal quantum dots (nQDs) were assembled and organized using microtubule (MT) filaments as nanoscale scaffolds.
nQD density and localization were systematically evaluated by varying the concentration and distribution of functional groups within the MT
structure. Confining nQD attachment to a central region within the MT enabled unaffected interaction with kinesin necessary to support active
transport of nQD−MT composites. This active transport system will be further refined to control the optical properties of a surface by regulating
the collective organization of nQD−MT composites.
Virus particles are captured and transported using kinesin‐driven, antibody‐functionalized microtubules. The functionalization was achieved through covalent crosslinking, which consequently enhanced the microtubule stability. The capture and transport of the virus particles was subsequently demonstrated in gliding motility assays in which antibody‐coated microtubules functioned as capture elements, and antibody‐coated microspheres served as fluorescent reporters (see Figure).
Chrysanthemyl diphosphate synthase (CPPase) catalyzes the condensation of two molecules of dimethylallyl diphosphate to produce chrysanthemyl diphosphate (CPP), a monoterpene with a non-head-to-tail or irregular c1-2-3 linkage between isoprenoid units. Irregular monoterpenes are common in Chrysanthemum cinerariaefolium and related members of the Asteraceae family. In C. cinerariaefolium, CPP is an intermediate in the biosynthesis of the pyrethrin ester insecticides. CPPase was purified from immature chrysanthemum flowers, and the N terminus of the protein was sequenced. A C. cinerariaefolium cDNA library was screened by using degenerate oligonucleotide probes based on the amino acid sequence to identify a CPPase clone that encoded a 45-kDa preprotein. The first 50 aa of the ORF constitute a putative plastidial targeting sequence. Recombinant CPPase bearing an N-terminal polyhistidine affinity tag in place of the targeting sequence was purified to homogeneity from an overproducing Escherichia coli strain by Ni 2؉ chromatography. Incubation of recombinant CPPase with dimethylallyl diphosphate produced CPP. The diphosphate ester was hydrolyzed by alkaline phosphatase, and the resulting monoterpene alcohol was analyzed by GC͞MS to confirm its structure. The amino acid sequence of CPPase aligns closely with that of the chain elongation prenyltransferase farnesyl diphosphate synthase rather than squalene synthase or phytoene synthase, which catalyze c1-2-3 cyclopropanation reactions similar to the CPPase reaction.
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