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• W2115038320 abstract "The dendritic architecture applied to peptides provides a practical entry into globular macromolecules resembling proteins. A modular design was chosen using a divergent synthesis on solid support alternating proteinogenic α-amino acids with branching diamino acids, producing peptide dendrimers with a molecular weight of 3−5 kDa. Initial studies focused on models for hydrolases and produced esterase peptide dendrimers featuring histidine as the key catalytic residue. Variations of amino acid composition and the branching diamino acid led to enantioselective catalysts. Rate accelerations of kcat/kuncat = 90 000 were obtained when the design was changed to monomeric peptide dendrimers alternating two amino acids with the branching unit. A combinatorial approach was developed allowing for the preparation of large libraries (>60 000 members), which were screened for B12 binding and catalytic activity. The peptide dendrimers were also investigated for drug delivery. Glycopeptide dendrimers conjugated to colchicine selectively inhibited the proliferation of targeted cells, whereas colchicine alone displayed high toxicity." @default.
• W2115038320 created "2016-06-24" @default.
• W2115038320 creator A5040229188 @default.
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• W2115038320 date "2006-08-31" @default.
• W2115038320 modified "2023-10-12" @default.
• W2115038320 title "Peptide Dendrimers as Artificial Enzymes, Receptors, and Drug-Delivery Agents" @default.
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• W2115038320 doi "https://doi.org/10.1021/ar050203y" @default.
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