Amphiphilic porphyrins, synthetic

Other templates have been described in the literature. Three independent groups used a porphyrin template. Sasaki and Kaiser utilized a porphyrin bearing four carboxylic acids (39) to prepare a synthetic metalloprotein with a four a-helix topology (40) [34], The utilization of a porphyrin template allows not only the templation of amphiphilic peptide segments, but also the incorporation of a metal binding site, which could serve eventually in a catalytic process (Fig. 16). 

Figure 9.6.10 A synthetic heme pocket. Both the peptide and the porphyrin react as bolaamphiphiles and as edge amphiphiles.

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