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题名: Binding studies of porphyrins to human serum albumin using affinity capillary electrophoresis
作者: Ding, YS;  Lin, BC;  Huie, CW
关键词: binding studies ;  porphyrins ;  human serum albumin ;  affinity capillary electrophoresis
刊名: ELECTROPHORESIS
发表日期: 2001-07-01
卷: 22, 期:11, 页:2210-2216
收录类别: ISTP ;  SCI
文章类型: Article
WOS标题词: Science & Technology ;  Life Sciences & Biomedicine ;  Physical Sciences
类目[WOS]: Biochemical Research Methods ;  Chemistry, Analytical
研究领域[WOS]: Biochemistry & Molecular Biology ;  Chemistry
英文摘要: The present work demonstrates that affinity capillary electrophoresis (ACE) can be employed as a valuable and powerful tool for studying the interactions between porphyrins and proteins in biological and biomedical research, such as the development of porphyrins and related compounds as efficient and selective photosensitizers in the photodynamic therapy of cancers. Binding constants of human serum albumin (HSA) to four biological porphyrins (uroporphyrin 1, heptacarboxylporphyrin, coproporphyrin I, protoporphyrin IX), which possess a wide range of hydrophobicity, were estimated by ACE. Based on 1:1 molecular association between these individual porphyrins and HSA, the change of the electrophoretic mobility of HSA as a function of porphyrin concentration in the run buffer was measured and the binding constants were calculated from the slope of the Scatchard plots. The binding constant values were found to be 8.80 +/- 0.51 x 10(4) m(-1), 2.39 +/- 0.16 x 10(5) m(-1), 1.61 +/- 0.11 x 10(6) m(-1), and 9.34 +/- 0.30 x 10(6) m(-1) for uroporphyrin I, heptacarboxylporphyrin, coproporphyrin I, and protoporphyrin IX, respectively, and most of these results are in good agreement with those reported in the literature using conventional methods for binding measurements. Additionally, experimental binding constant data obtained using ACE was found to exhibit very good correlation with theoretical hydrophobicity values calculated using the Rekker's hydrophobic fragmental constant method, thus further supporting the hypothesis that the hydrophobicity of the porphyrin side chains play an important role in governing the hydrophobic interaction of porphyrins with serum proteins such as HSA.
语种: 英语
WOS记录号: WOS:000170175800013
Citation statistics: 
内容类型: 期刊论文
URI标识: http://cas-ir.dicp.ac.cn/handle/321008/138993
Appears in Collections:中国科学院大连化学物理研究所_期刊论文

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作者单位: 1.Hong Kong Baptist Univ, Dept Chem, Kowloon Tong, Hong Kong, Peoples R China
2.Chinese Acad Sci, Dalian Inst Chem Phys, Dalian, Peoples R China

Recommended Citation:
Ding, YS,Lin, BC,Huie, CW. Binding studies of porphyrins to human serum albumin using affinity capillary electrophoresis[J]. ELECTROPHORESIS,2001,22(11):2210-2216.
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