Influence of molecular structure on O2-binding properties and blood circulation of hemoglobin?albumin clusters

Kana Yamada, Kyoko Yokomaku, Risa Haruki, Kazuaki Taguchi, Saori Nagao, Toru Maruyama, Masaki Otagiri, Teruyuki Komatsu

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

A hemoglobin wrapped covalently by three human serum albumins, a Hb-HAS3 cluster, is an artificial O2-carrier with the potential to function as a red blood cell substitute. This paper describes the synthesis and O2-binding properties of new hemoglobin?albumin clusters(i) bearing four HSA units at the periphery(Hb-HSA4, large-size variant) and(ii) containing an intramolecularly crosslinked Hb in the center(XLHb-HSA3, high O2-affinity variant). Dynamic light scattering measurements revealed that the Hb-HSA4 diameter is greater than that of either Hb-HSA3 or XLHb-HSA3. The XLHb-HSA3 showed moderately high O2-affinity compared to the others because of the chemical linkage between the Cys-93(β) residues in Hb. Furthermore, the blood circulation behavior of 125I-labeled clusters was investigated by assay of blood retention and tissue distribution after intravenous administration into anesthetized rats. The XLHb-HSA3 was metabolized faster than Hb-HSA3 and Hb-HSA4. Results suggest that the molecular structure of the protein cluster is a factor that can influence in vivo circulation behavior.

Original languageEnglish
Article numbere0149526
JournalPLoS One
Volume11
Issue number2
DOIs
Publication statusPublished - 2016 Feb 1
Externally publishedYes

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Blood Substitutes
blood circulation
binding properties
Blood Circulation
Hemodynamics
Molecular Structure
chemical structure
Molecular structure
albumins
Albumins
hemoglobin
Hemoglobins
Blood
Bearings (structural)
tissue distribution
light scattering
Dynamic light scattering
Tissue Distribution
intravenous injection
Serum Albumin

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)

Cite this

Influence of molecular structure on O2-binding properties and blood circulation of hemoglobin?albumin clusters. / Yamada, Kana; Yokomaku, Kyoko; Haruki, Risa; Taguchi, Kazuaki; Nagao, Saori; Maruyama, Toru; Otagiri, Masaki; Komatsu, Teruyuki.

In: PLoS One, Vol. 11, No. 2, e0149526, 01.02.2016.

Research output: Contribution to journalArticle

Yamada, K, Yokomaku, K, Haruki, R, Taguchi, K, Nagao, S, Maruyama, T, Otagiri, M & Komatsu, T 2016, 'Influence of molecular structure on O2-binding properties and blood circulation of hemoglobin?albumin clusters', PLoS One, vol. 11, no. 2, e0149526. https://doi.org/10.1371/journal.pone.0149526
Yamada, Kana ; Yokomaku, Kyoko ; Haruki, Risa ; Taguchi, Kazuaki ; Nagao, Saori ; Maruyama, Toru ; Otagiri, Masaki ; Komatsu, Teruyuki. / Influence of molecular structure on O2-binding properties and blood circulation of hemoglobin?albumin clusters. In: PLoS One. 2016 ; Vol. 11, No. 2.
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