Static structures and dynamics of hemoglobin vesicle (HbV) developed as a transfusion alternative

Takaaki Sato, Hiromi Sakai, Keitaro Sou, Martin Medebach, Otto Glatter, Eishun Tsuchida

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

Hemoglobin vesicle (HbV) is an artificial oxygen carrier that encapsulates solution of purified and highly concentrated (ca. 38 g dL-1) human hemoglobin. Its exceptionally high concentration as a liposomal product (ca. 40% volume fraction) achieves an oxygen-carrying capacity comparable to that of blood. We use small-angle X-ray scattering (SAXS) and dynamic light scattering (DLS) to investigate the hierarchical structures and dynamics of HbVs in concentrated suspensions. SAXS data revealed unilamellar shell structure and internal density profile of the artificial cell membrane for Hb encapsulation. The SAXS intensity of HbV at scattering vector q > 0.5 nm-1 manifests dissolution states of the encapsulated Hbs in the inner aqueous phase of the vesicle having ca. 240 nm diameter. The peak position as well as the height and width of static structure factor of Hb before and after encapsulation are almost identical, demonstrating the preserved protein-protein interactions in the confined space. To overcome multiple scattering from turbid samples, we employed thin layer-cell DLS combined with the so-called bruteforce and echo techniques, which allows us to observe collective diffusion dynamics of HbVs without dilution. A pronounced slowdown of the HbV diffusion and eventual emergence of dynamically arrested state in the presence of high-concentration plasma substitutes (water-soluble polymers), such as dextran, modified fluid gelatin, and hydroxylethyl starch, can be explained by depletion interaction. A significantly weaker effect of recombinant human serum albumin on HbV flocculation and viscosity enhancement than those induced by other polymers is clearly attributed to the specificity as a protein; its compact structure efficiently reduces the reservoir polymer volume fraction that determines the depth of the attractive potential between HbVs. These phenomena are technically essential for controlling the suspension rheology, which is advantageous for versatile clinical applications.

Original languageEnglish
Pages (from-to)8418-8428
Number of pages11
JournalJournal of Physical Chemistry B
Volume113
Issue number24
DOIs
Publication statusPublished - 2009 Jun 18

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transfusion
Hemoglobin
hemoglobin
Hemoglobins
X ray scattering
scattering
Polymers
Dynamic light scattering
proteins
Proteins
Encapsulation
Volume fraction
Suspensions
polymers
light scattering
Plasma Substitutes
Oxygen
dextrans
x rays
Dextran

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Materials Chemistry
  • Surfaces, Coatings and Films

Cite this

Static structures and dynamics of hemoglobin vesicle (HbV) developed as a transfusion alternative. / Sato, Takaaki; Sakai, Hiromi; Sou, Keitaro; Medebach, Martin; Glatter, Otto; Tsuchida, Eishun.

In: Journal of Physical Chemistry B, Vol. 113, No. 24, 18.06.2009, p. 8418-8428.

Research output: Contribution to journalArticle

Sato, T, Sakai, H, Sou, K, Medebach, M, Glatter, O & Tsuchida, E 2009, 'Static structures and dynamics of hemoglobin vesicle (HbV) developed as a transfusion alternative', Journal of Physical Chemistry B, vol. 113, no. 24, pp. 8418-8428. https://doi.org/10.1021/jp9002142
Sato, Takaaki ; Sakai, Hiromi ; Sou, Keitaro ; Medebach, Martin ; Glatter, Otto ; Tsuchida, Eishun. / Static structures and dynamics of hemoglobin vesicle (HbV) developed as a transfusion alternative. In: Journal of Physical Chemistry B. 2009 ; Vol. 113, No. 24. pp. 8418-8428.
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