Peroxidase-like oxidative activity of a manganese-coordinated histidyl bolaamphiphile self-assembly

Min Chul Kim, Sang Yup Lee

Research output: Contribution to journalArticlepeer-review

35 Citations (Scopus)


A peroxidase-like catalyst was constructed through the self-assembly of histidyl bolaamphiphiles coordinated to Mn2+ ions. The prepared catalyst exhibited oxidation activity for the organic substrate o-phenylenediamine (OPD) in the presence of hydrogen peroxide (H2O2). The histidyl bolaamphiphiles of bis(N-alpha-amido-histidine)-1,7-heptane dicarboxylates self-assembled to make spherical structures in an aqueous solution. Subsequent association of Mn2+ ions with the histidyl imidazoles in the self-assembly produced catalytic active sites. The optimal Mn2+ ion concentration was determined and coordination of the Mn2+ ion with multiple histidine imidazoles was investigated using spectroscopy analysis. The activation energy of the produced catalysts was 55.0 kJ mol-1, which was comparable to other peroxidase-mimetic catalysts. A detailed kinetics study revealed that the prepared catalyst followed a ping-pong mechanism and that the turnover reaction was promoted by increasing the substrate concentration. Finally, application of the prepared catalyst for glucose detection was demonstrated through cascade enzyme catalysis. This study demonstrated a facile way to prepare an enzyme-mimetic catalyst through the self-assembly of an amphiphilic molecule containing amino acid segments.

Original languageEnglish
Pages (from-to)17063-17070
Number of pages8
Issue number40
Publication statusPublished - 2015 Oct 28

Bibliographical note

Publisher Copyright:
© 2015 The Royal Society of Chemistry.

All Science Journal Classification (ASJC) codes

  • Materials Science(all)


Dive into the research topics of 'Peroxidase-like oxidative activity of a manganese-coordinated histidyl bolaamphiphile self-assembly'. Together they form a unique fingerprint.

Cite this