closo-Boranes as Structural Elements for Liquid Crystals

Boron Science ◽  
2011 ◽  
pp. 319-354 ◽  
Author(s):  
Piotr Kaszynski
Author(s):  
M. Locke ◽  
J. T. McMahon

The fat body of insects has always been compared functionally to the liver of vertebrates. Both synthesize and store glycogen and lipid and are concerned with the formation of blood proteins. The comparison becomes even more apt with the discovery of microbodies and the localization of urate oxidase and catalase in insect fat body.The microbodies are oval to spherical bodies about 1μ across with a depression and dense core on one side. The core is made of coiled tubules together with dense material close to the depressed membrane. The tubules may appear loose or densely packed but always intertwined like liquid crystals, never straight as in solid crystals (Fig. 1). When fat body is reacted with diaminobenzidine free base and H2O2 at pH 9.0 to determine the distribution of catalase, electron microscopy shows the enzyme in the matrix of the microbodies (Fig. 2). The reaction is abolished by 3-amino-1, 2, 4-triazole, a competitive inhibitor of catalase. The fat body is the only tissue which consistantly reacts positively for urate oxidase. The reaction product is sharply localized in granules of about the same size and distribution as the microbodies. The reaction is inhibited by 2, 6, 8-trichloropurine, a competitive inhibitor of urate oxidase.


Author(s):  
Jun Jiao

HREM studies of the carbonaceous material deposited on the cathode of a Huffman-Krätschmer arc reactor have shown a rich variety of multiple-walled nano-clusters of different shapes and forms. The preparation of the samples, as well as the variety of cluster shapes, including triangular, rhombohedral and pentagonal projections, are described elsewhere.The close registry imposed on the nanotubes, focuses attention on the cluster growth mechanism. The strict parallelism in the graphitic separation of the tube walls is maintained through changes of form and size, often leading to 180° turns, and accommodating neighboring clusters and defects. Iijima et. al. have proposed a growth scheme in terms of pentagonal and heptagonal defects and their combinations in a hexagonal graphitic matrix, the first bending the surface inward, and the second outward. We report here HREM observations that support Iijima’s suggestions, and add some new features that refine the interpretation of the growth mechanism. The structural elements of our observations are briefly summarized in the following four micrographs, taken in a Hitachi H-8100 TEM operating at an accelerating voltage of 200 kV and with a point-to-point resolution of 0.20 nm.


2003 ◽  
Vol 70 ◽  
pp. 201-212 ◽  
Author(s):  
Hideaki Nagase ◽  
Keith Brew

The tissue inhibitors of metalloproteinases (TIMPs) are endogenous inhibitors of the matrix metalloproteinases (MMPs), enzymes that play central roles in the degradation of extracellular matrix components. The balance between MMPs and TIMPs is important in the maintenance of tissues, and its disruption affects tissue homoeostasis. Four related TIMPs (TIMP-1 to TIMP-4) can each form a complex with MMPs in a 1:1 stoichiometry with high affinity, but their inhibitory activities towards different MMPs are not particularly selective. The three-dimensional structures of TIMP-MMP complexes reveal that TIMPs have an extended ridge structure that slots into the active site of MMPs. Mutation of three separate residues in the ridge, at positions 2, 4 and 68 in the amino acid sequence of the N-terminal inhibitory domain of TIMP-1 (N-TIMP-1), separately and in combination has produced N-TIMP-1 variants with higher binding affinity and specificity for individual MMPs. TIMP-3 is unique in that it inhibits not only MMPs, but also several ADAM (a disintegrin and metalloproteinase) and ADAMTS (ADAM with thrombospondin motifs) metalloproteinases. Inhibition of the latter groups of metalloproteinases, as exemplified with ADAMTS-4 (aggrecanase 1), requires additional structural elements in TIMP-3 that have not yet been identified. Knowledge of the structural basis of the inhibitory action of TIMPs will facilitate the design of selective TIMP variants for investigating the biological roles of specific MMPs and for developing therapeutic interventions for MMP-associated diseases.


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