Dendrimers peptide/polypeptide

This volume focuses on extensions of peptide chemistry into the novel areas of template-conjugated peptides, helical arrays of polypeptides, dendrimers, and C-terminally modified peptides. The volume concludes with an overview of the classic syntheses of representative peptide natural products. 

In recent work Tam and Rao have attached unprotected peptides directly to a third generation poly(a, -L-lysine) dendrimer [149]. As shown in Scheme 20b, the dendrimer is modified to contain eight aldehyde groups. These are then reacted with a cysteine terminated polypeptide with formation of a thiazolidine ring. The addition of the first five polypeptides occurs within 2 h at 18 °C but addition of subsequent peptide chains becomes progressively slower. After 67 h a... 

Rao and Tam[19 reported the connection of a 24-residue peptide to a small, lysine-based dendrimer (Scheme 7.3). The peptide connection was effected via treatment of the octameric, glyoxylyl-terminated dendrimer 15 with the 1,2-aminothiol polypeptide 16 to afford the thiazolidinyl peptide dendrimer 17. The thiazolidine linkage also introduces a new asymmetric center. 

It is known that proteins can incorporate porphyrin units by embedded them into their peptidic frameworks [170]. With such systems, the polypeptidic shells modulate the response of the porphyrin units to the external environment. Non-natural counterparts of these biologically occurring systems can be generated by embedding one or more porphyrin systems inside dendritic frameworks. Indeed, several dendrimers incorporating porphyrin cores have been designed and synthesized already [171,172]. 

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