Hemodextrin: A self-assembled cyclodextrin-porphyrin construct that binds dioxygen

Huchen Zhou, John Taylor Groves

Research output: Contribution to journalArticle

17 Scopus citations

Abstract

Synthetic hemoprotein model compounds are of great interest due to the vital roles and complexities of hemoproteins. This study reports a novel, self-assembled hemoprotein model, hemodextrin. The synthesis and characterization of py-PPCD (2A-monopyridylmethyl-perPEGylated-β -cyclodextrin) (2) is described. The molecular design is based on a pegylated cyclodextrin scaffold that bears both a heme-binding pocket and an axial ligand that binds an iron porphyrin. The binding constant for Fe(III)TPPS [iron(III) meso-tetra(4-sulphonatophenyl)porphyrin] by py-PPCD (2) was determined to be 2×106 M-1 at pH 6.0 by observing characteristic changes in the UV-Vis spectrum of the porphyrin. The pyridyl nitrogen of py-PPCD (2) was shown to ligate to the iron center by observing signal changes in the Fe(II)-porphyrin 1H-NMR spectrum. This hemodextrin ensemble was shown to bind dioxygen reversibly and to form a stable ferryl species.

Original languageEnglish (US)
Pages (from-to)639-648
Number of pages10
JournalBiophysical Chemistry
Volume105
Issue number2-3
DOIs
StatePublished - Sep 1 2003

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Organic Chemistry

Keywords

  • Cyclodextrin
  • Hemoprotein
  • Porphyrin
  • Self-assembly

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