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将血红蛋白捕获于刚性基质中:通过调节封装方案对氧结合特性进行微调。

Trapping hemoglobin in rigid matrices: fine tuning of oxygen binding properties by modulation of encapsulation protocols.

作者信息

Bruno Stefano, Ronda Luca, Bettati Stefano, Mozzarelli Andrea

机构信息

Department of Biochemistry and Molecular Biology, University of Parma, Parma, Italy.

出版信息

Artif Cells Blood Substit Immobil Biotechnol. 2007;35(1):69-79. doi: 10.1080/10731190600974541.

DOI:10.1080/10731190600974541
PMID:17364472
Abstract

Encapsulation of hemoglobin in a biocompatible matrix is a potential strategy for obtaining blood substitutes. Such a system would retain most of the immunogenic and functional properties of the physiologically relevant oxygen carrier but would prevent protein extravasation and dimer/dimer dissociation. We applied this approach by entrapping hemoglobin in wet nanoporous silica gel, in the presence and absence of allosteric effectors. Silica gels, although not suitable for intravenous perfusion, are inert and optically transparent, thus allowing a full characterization of the functional and structural properties of encapsulated hemoglobin by spectroscopic techniques. Results indicate that hemoglobin molecules, entrapped using different protocols, exhibit an oxygen affinity that can be modulated between 12 and 140 torr. This tunability could be exploited to meet distinct clinical needs.

摘要

将血红蛋白包裹在生物相容性基质中是获得血液替代品的一种潜在策略。这样的系统将保留生理相关氧载体的大部分免疫原性和功能特性,但可防止蛋白质外渗和二聚体/二聚体解离。我们通过在存在和不存在变构效应剂的情况下将血红蛋白包埋在湿纳米多孔硅胶中来应用此方法。硅胶虽然不适合静脉灌注,但具有惰性且光学透明,因此可以通过光谱技术全面表征包封血红蛋白的功能和结构特性。结果表明,使用不同方案包埋的血红蛋白分子表现出的氧亲和力可在12至140托之间调节。这种可调性可用于满足不同的临床需求。

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