Metalloporphyrin receptors for histidine-containing peptides

Two new ditopic metalloporphyrin receptors constructed by combining metalloporphyrin with crown ethers have been prepared and characterized. 1H NMR and MS spectra confirmed the complexation of receptor with peptide driven by coordination interaction and hydrogen bonding. UV/vis experiments revealed that the receptors exhibited high binding affinity to histidine-containing peptides. These receptors could differentiate short peptides of C-terminal histidine and N-terminal histidine and formed the most stable complexes with tripeptide.

Two new ditopic metalloporphyrin receptors, which were constructed by the combination of metalloporphyrin and crown ethers, have been prepared and characterized. They showed length- and sequence-selectivity toward histidine-containing peptides.Figure optionsDownload as PowerPoint slide