Haemoglobin site-specifically modified with ferulic acid to suppress the autoxidation

Qi, Donglai; Li, Qian; Wang, Pei; Wang, Xiang

doi:10.1080/21691401.2017.1309659

Cited by 4 publications

(3 citation statements)

References 28 publications

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“…HBOCs in practice were expected to maintain stability in long production and storage processes . However, in the absence of an antioxidant system, including superoxide dismutase (SOD), catalase (CAT), and glutathione (GSH) , the heme iron of Hb is easily oxidized to the ferric state (methemoglobin, metHb), which cannot carry oxygen . Therefore, research on oxidation is essential to improve the capability of Hb as an HBOC.…”

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confidence: 99%

Study on Oxidation Stability and Oxygen Affinity of Hemoglobin During Storage

Zhang

et al. 2018

Artificial Organs

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The factors affecting hemoglobin (Hb) oxidation in its short- and long-term storage were investigated. Porcine Hb with different levels of oxygen saturation was stored at 25°C or 4°C for 40 days. The methemoglobin (metHb) content increased rapidly when Hb was at half saturation with oxygen at 4°C, increased gradually with the increase in Hb oxygenation or deoxygenation, and was almost unchanged when Hb was highly oxygenated or deoxygenated. The Hb oxidation was more intense when stored at 25°C. This indicated that highly oxygenated or deoxygenated Hb can be stored short term at 4°C. The accelerated test showed that metHb content was almost unchanged when Hb was highly deoxygenated and stored at 37°C for 7 days; however, the metHb content rapidly increased when Hb was highly oxygenated and stored at 37°C, which indicated that only highly deoxygenated Hb is suitable for long-term storage. Then, the long-term oxidation stability of highly deoxygenated Hb and polymerized hemoglobin was verified; the metHb content of both did not show significant changes at 4°C for 18 months. Moreover, the results in this work indicated that a temperature increasing from 20 to 40°C clearly increased the partial oxygen pressure (P50), which represents decreased oxygen affinity and is beneficial to deoxygenation. Furthermore, P50 was increased when the pH decreased from 9 to 7. Therefore, we concluded that the appropriate high temperature and neutral condition in vitro are conducive to reducing the oxygen affinity of Hb to achieve efficient deoxygenation, which could promote the development of hemoglobin-based oxygen carriers.

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confidence: 99%

Study on Oxidation Stability and Oxygen Affinity of Hemoglobin During Storage

Zhang

et al. 2018

Artificial Organs

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“…Human blood solution was separately washed with an equivalent amount of saline and centrifuged (2000 g, 10 min) three times to yield a concentrated RBC suspension [11]. The preparation of purified Hb from human umbilical cord blood was referred to the methods described by Walder et al [12] and Qi et al [13]. The final product in the retentate was collected and stored at À80 C. The concentration of the purified Hb was determined with SLS-Hb (sodium lauryl sulfate-Hb) method [14].…”

Section: Preparation Of Rbcs Suspension and Purification Of Hb From Rbcsmentioning

confidence: 99%

Kinetic studies on oxygen releasing of HBOC and red blood cells as fluids and factors affecting the process

Zhao

Zhang

Meng

et al. 2018

Artificial Cells, Nanomedicine, and Biotechnology

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Red blood cells (RBCs) possess intact cyto-architectures while haemoglobin (Hb) is a cell-free, homogeneous solution. Both RBCs and Hb are generalized oxygen carriers. In this paper, kinetic studies on oxygen-releasing of high concentration of Hb and RBCs under various conditions were carried out regarding Hb and RBCs as fluids. Among them, Hb under specific conditions was seen as the simplest Hb-based oxygen carrier (HBOC), Also, factors affecting the oxygen releasing of Hb and RBCs, including osmotic pressure, viscosity and allosteric agent, have been well studied. Analysis of the results from the measurement above showed that kinetics of oxygen releasing of either pure Hb or the simplest HBOCs was obviously different from that of RBCs. The oxygen-releasing time of Hb was shorter and the oxygen-releasing rates of Hb were quicker than those of RBCs under various conditions. Therefore, as fluids, only by changing the milieus it exists in, Hb could not achieve the expected oxygen-releasing effect on the microcirculation so well as RBCs do in the same system, irrespective of the interaction between the fluids and blood vessels. Furthermore, kinetic properties of HBOCs must be considered and matched with those of RBCs in the study of HBOCs.

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“…Moreover, its use entails various complicated, time-consuming and expensive blood tests, creating persistent conditions of blood supply shortage. Alternative blood substitutes such as haemoglobinbased oxygen carriers (HBOCs) are believed to have the capacity to ease blood supply shortages and alleviate many blood transfusion-related issues [1][2][3][4][5][6]. Actually, HBOCs can be produced in a way that eliminates viral infections such as HIV and hepatitis.…”

Section: Introductionmentioning

confidence: 99%

In vivoevaluation of electron mediators for the reduction of methemoglobin encapsulated in liposomes using electron energies produced by red blood cell glycolysis

Ghirmai

Bülow

Sakai

2017

Artificial Cells, Nanomedicine, and Biotechnology

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Earlier studies have clarified that NADH and NADPH, re-energized repeatedly by red blood cell (RBC) glycolysis, can be used in extracellular chemical reactions, where electron energies are extracted by electron mediators, such as methylene blue (MB). The electron mediators, which are reduced by NAD(P)H, permeate both the membranes of RBC and phospholipid bilayer of liposomes encapsulating haemoglobin (Hb-vesicles, HbV) and reduce autoxidized ferric methemoglobin (metHb) in HbV to ferrous Hb. Moreover, in vitro screening study clarified some other potential electron mediators with comparable capacity to reduce metHb. Given this background, eight of these compounds: MB, 1,9-dimethyl MB, azure A, azure B (AB), azure, toluidine blue, brilliant cresyl blue and toluylene blue, were evaluated in both in vitro and in vivo studies in this work. Compared with MB as a reference, in vitro experiments demonstrated that most compounds caused effective metHb reduction of HbV in the presence of RBC. However, in vivo experiments of bolus injection of autoxidized HbV to rats (10 mL HbV/kg body weight) followed by injection of the dye (1.53 mL/kg body weight, 2.6 mM) led to some differences from in vitro results. Effective metHb reduction was found for the combination of AB. To evaluate AB effectiveness further, a haemorrhagic shock and resuscitation model was used, where the rats were resuscitated with HbV. When the level of metHb increased to 50%, a dye solution was injected. Again, AB caused sufficient reduction of metHb. Through these in vivo experiments, this study clarified that AB is a suitable electron mediator to prolong the functional lifetime of HbV.

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Haemoglobin site-specifically modified with ferulic acid to suppress the autoxidation

Cited by 4 publications

References 28 publications

Study on Oxidation Stability and Oxygen Affinity of Hemoglobin During Storage

Study on Oxidation Stability and Oxygen Affinity of Hemoglobin During Storage

Kinetic studies on oxygen releasing of HBOC and red blood cells as fluids and factors affecting the process

In vivoevaluation of electron mediators for the reduction of methemoglobin encapsulated in liposomes using electron energies produced by red blood cell glycolysis

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