269411-88-3Relevant articles and documents
Modular Approach to the Accelerated Convergent Growth of Laser Dye-Labeled Poly(aryl ether) Dendrimers Using a Novel Hypermonomer
Gilat, Sylvain L.,Adronov, Alex,Frechet, Jean M. J.
, p. 7474 - 7484 (1999)
The synthesis of novel dendrimers functionalized with laser dyes both at the periphery and at the core, along with all relevant model compounds necessary for accurate photophysical studies, is described. The utilized synthetic strategy involves a modular approach in which a variety of peripheral and core moieties can be placed on a dendritic structure bearing electrophilic peripheral groups and a nucleophilic core. Specifically, the target macromolecules required functionalization with the laser dyes coumarin 2 (periphery) and coumarin 343 (core) due to the possibility of energy transfer from the former to the latter dye. In addition, the preparation of a novel, highly soluble and reactive hypermonomer utilized in the rapid and efficient synthesis of high-generation dye-labeled dendrimers and model compounds is outlined.
Synthesis and supramolecular properties of a novel octaphosphonate porphyrin
Bhosale, Sheshanath V.,Kalyankar, Mohan B.,Langibrd, Steven J.,Bhosale, Sidhanath V.,Oliver, Ruth F.
experimental part, p. 4128 - 4134 (2009/12/26)
Two complementary routes were developed for preparing novel octaphosphonate porphyrins. The use of protected/deprotected phosphonate-substituted precursors in the rational synthesis gave an overall yield 16%. A more streamlined synthetic path gave 21 % overall yield, of the target molecule. Octaphosphonate porphyrin possesses promising properties in supramolecular aggregate formation with cyclam. Cofacial reversible self-assembly of a meso-substituted octaphosphonate porphyrin with cyclam yields micrometer-long nanowires with a height of about 1-1.5 nm. The resulting wires were characterized by UV/Vis absorption, emission and atomic force microscopy and transmission electron microscopy. ( Wiley-VCH Verlag GmbH & Co. KGaA.
Substituted benzamide inhibitors of rhinovirus 3C protease
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Page column 19, (2010/01/31)
Nonpeptide benzamide-containing inhibitors of human rhinovirus (HRV) 3C protease are described.
Substituted benzamide inhibitors of human rhinovirus 3C protease: Structure-based design, synthesis, and biological evaluation
Reich, Siegfried H.,Johnson, Theodore,Wallace, Michael B.,Kephart, Susan E.,Fuhrman, Shella A.,Worland, Stephen T.,Matthews, David A.,Hendrickson, Thomas F.,Chan, Fora,Meador III, James,Ferre, Rose Ann,Brown, Edward L.,DeLisle, Dorothy M.,Patick, Amy K.,Binford, Susan L.,Ford, Clifford E.
, p. 1670 - 1683 (2007/10/03)
A series of nonpeptide benzamide-containing inhibitors of human rhinovirus (HRV) 3C protease was identified using structure-based design. The design, synthesis, and biological evaluation of these inhibitors are reported. A Michael acceptor was combined with a benzamide core mimicking the P1 recognition element of the natural 3CP substrate, α,β-Unsaturated cinnamate esters irreversibly inhibited the 3CP and displayed antiviral activity (EC50 0.60/μM, HRV-16 infected H1-HeLa cells). On the basis of cocrystal structure information, a library of substituted benzamide derivatives was prepared using parallel synthesis on solid support. A 1.9 A? cocrystal structure of a benzamide inhibitor in complex with the 3CP revealed a binding mode similar to that initially modeled wherein covalent attachment of the nucleophilic cysteine residue is observed. Unsaturated ketones displayed potent reversible inhibition but were inactive in the cellular antiviral assay and were found to react with nucleophilic thiols such as DTT.
