Journal of medicinal chemistry, 45(10), 1971-1982 (2002-05-03)
A one-bead-two-compound inhibitor library was synthesized by the split-mix method for the identification of inhibitors of a recombinant cysteine protease from Leishmania mexicana, CPB2.8DeltaCTE. The inhibitor library was composed of octapeptides with a centrally located reduced bond introduced by reductive
Various modifications of alginate-poly-L-lysine microcapsules were made, such as the inclusion of polyethylenimine (PEI) or carboxyl methyl cellulose (CMC) in the core and the coating of bis(polyoxyethylene bis[amine]) (PEGA) onto the microcapsule membrane surface. A characterization of the modified microcapsules
The synthesis and olefin metathesis activity in protic solvents of 7, a phosphine-free ruthenium alkylidene bound to a hydrophilic solid support are reported. This heterogeneous catalyst promotes relatively efficient ring closing- and cross-metathesis reactions in both methanol and water. The
The design of hydrogels that simultaneously report protease activity and remove excess protease from solution is elucidated. The hydrogels, based on amino-PEGA, combine enzyme-specific peptides flanked with FRET complimented by charged amino acid residues that facilitate protease uptake via short
Highlighting new synthetic modifications of PEG to improve the mechanical properties and degradation of resulting hydrogels in tissue engineering applications.
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