O2-binding properties of albumin hybrid incorporating porphyrinatoiron having histidine derivative

Akito Nakagawa, Teruyuki Komatsu, Eishun Tsuchida, Makoto Iiduka, Shinji Takeoka

Research output: Contribution to conferencePaper

Abstract

We have evaluated the dioxygen binding properties of albumin hybrid incorporating porphyrinatoirons having histidine derivative [FeP(His), FeP(MHis)]. They were synthesized via 9 steps from 5,10,15,20-tetrakis(o- aminophenyl)porphyrin. FeP(His) binds histidine and FeP(MHis) binds 1-methylhistidine as a proximal base. Both hemes could be incorporated into human serum albumin (HSA) providing HSA hybrid [HSA-FeP(His) or HSA-FeP(MHis)] in the buffer solution (pH 7.3). HSA-FeP(MHis) showed a low O 2-binding affinity (P50: 15 Torr) and a high O 2-dissociation rate constant in comparison to HSA-FeP(His). This is due to the steric hindrance for the coordination of the proximal base derived from the methylene group at 4-posititon of imidazole ring in FeP(MHis). HSA-FeP(MHis) can be utilized as a new artificial O2-therapeutics.

Original languageEnglish
Number of pages1
Publication statusPublished - 2006 Dec 1
Event55th Society of Polymer Science Japan Symposium on Macromolecules - Toyama, Japan
Duration: 2006 Sep 202006 Sep 22

Other

Other55th Society of Polymer Science Japan Symposium on Macromolecules
CountryJapan
CityToyama
Period06/9/2006/9/22

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Keywords

  • Albumin
  • Artificial blood
  • Heme
  • Hemoprotein
  • Porphyrin

ASJC Scopus subject areas

  • Engineering(all)

Cite this

Nakagawa, A., Komatsu, T., Tsuchida, E., Iiduka, M., & Takeoka, S. (2006). O2-binding properties of albumin hybrid incorporating porphyrinatoiron having histidine derivative. Paper presented at 55th Society of Polymer Science Japan Symposium on Macromolecules, Toyama, Japan.