中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
CO binding improves the structural, functional, physical and anti-oxidation properties of the PEGylated hemoglobin

文献类型:期刊论文

作者Wang, Q. Q.; Hu, T.; Sun, L. J.; Ji, S. Y.; Zhao, D. W.; Liu, J. X.; Ma, G. H.; Su, Z. G.
刊名Artificial Cells Nanomedicine and Biotechnology
出版日期2015
期号1页码:18-25
关键词autoxidation heme environment oxygen carrier PEGylation thermal stability CARBONMONOXY HEMOGLOBIN CIRCULAR-DICHROISM IN-VITRO PEG-HB DISSOCIATION CONJUGATE MP4 CARRIER LINKER SITES
其他题名Artif. Cell. Nanomed. Biotechnol.
中文摘要Context: PEGylated hemoglobin (Hb) is a promising oxygen therapeutic agent for clinical application. However, it suffered from structural perturbation, functional instability and methemoglobin (metHb) formation. Objective: To improve the structural, functional, physical and anti-oxidation properties of the PEGylated Hb. Materials and methods: PEGylation of Hb with CO binding (HbCO) was conducted using maleimide and acylation chemistry, respectively. Physical and chemical parameters were measured for Hb samples. The circular dichroism spectra, dynamic light scattering and analytical ultracentrifugation were used to investigate the structure and conformation of PEGylated HbCO. Results: CO binding can inhibit the autoxidation of the PEGylated Hb, structurally stabilize its tetramer and improve its thermal and pH stability. Importantly, the circular dichroism spectra showed that CO binding can decrease the structural perturbation of Hb induced by PEGylation. The PEGylated HbCO with CO release showed slightly higher oxygen-delivery capacity than the PEGylated Hb. The PEGylated HbCO did not show metHb formation after 30-day storage at 4 degrees C. Discussion and conclusion: CO binding structurally stabilized the PEGylated Hb, abolished its metHb formation, and significantly increased its physical stability. In particular, it also avoided the perturbation of PEG chains on the heme microenvironment. The functional property of the PEGylated HbCO can be maintained during its long-term storage, which is of great significance for field transfusion.
收录类别SCI
原文出处://WOS:000347531900003
语种英语
WOS记录号WOS:000347531900003
公开日期2015-04-01
源URL[http://ir.ipe.ac.cn/handle/122111/11847]  
专题过程工程研究所_研究所(批量导入)
推荐引用方式
GB/T 7714
Wang, Q. Q.,Hu, T.,Sun, L. J.,et al. CO binding improves the structural, functional, physical and anti-oxidation properties of the PEGylated hemoglobin[J]. Artificial Cells Nanomedicine and Biotechnology,2015(1):18-25.
APA Wang, Q. Q..,Hu, T..,Sun, L. J..,Ji, S. Y..,Zhao, D. W..,...&Su, Z. G..(2015).CO binding improves the structural, functional, physical and anti-oxidation properties of the PEGylated hemoglobin.Artificial Cells Nanomedicine and Biotechnology(1),18-25.
MLA Wang, Q. Q.,et al."CO binding improves the structural, functional, physical and anti-oxidation properties of the PEGylated hemoglobin".Artificial Cells Nanomedicine and Biotechnology .1(2015):18-25.

入库方式: OAI收割

来源:过程工程研究所

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