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Protoporphyrin IX-induced structural and functional changes in human red blood cells, haemoglobin and myoglobin
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  • 作者:Susmita Sil ; Tania Bose ; Dibyendu Roy ; Abhay Sankar Chakraborti
  • 关键词:Drug ; protein binding ; haemoglobin ; myoglobin ; protoporphyrin IX ; red blood cells
  • 刊名:Journal of Biosciences
  • 出版年:2004
  • 出版时间:September 2004
  • 年:2004
  • 卷:29
  • 期:3
  • 页码:281-291
  • 全文大小:
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  • 作者单位:Susmita Sil (1)
    Tania Bose (1)
    Dibyendu Roy (1)
    Abhay Sankar Chakraborti (1)

    1. Department of Biophysics, Molecular Biology and Genetics, University College of Science, 92, Acharyya Prafulla Chandra Road, 700 009, Kolkata, India
  • 刊物类别:Life Sciences, general; Biomedicine general; Zoology; Plant Sciences; Microbiology; Cell Biology;
  • 刊物主题:Life Sciences, general; Biomedicine general; Zoology; Plant Sciences; Microbiology; Cell Biology;
  • 出版者:Springer India
  • ISSN:0973-7138
文摘
Protoporphyrin IX and its derivatives are used as photosensitizers in the photodynamic therapy of cancer. Protoporphyrin IX penetrates into human red blood cells and releases oxygen from them. This leads to a change in the morphology of the cells. Spectrophotometric studies reveal that protoporphyrin IX interacts with haemoglobin and myoglobin forming ground state complexes. For both proteins, the binding affinity constant decreases, while the possible number of binding sites increases, as the aggregation state of the porphyrin is increased. The interactions lead to conformational changes of both haemoglobin and myoglobin as observed in circular dichroism studies. Upon binding with the proteins, protoporphyrin IX releases the heme-bound oxygen from the oxyproteins, which is dependent on the stoichiometric ratios of the porphyrin: protein. The peroxidase activities of haemoglobin and myoglobin are potentiated by the protein-porphyrin complexation. Possible mechanisms underlying the relation between the porphyrin-induced structural modifications of the heme proteins and alterations in their functional properties have been discussed. The findings may have a role in establishing efficacy of therapeutic uses of porphyrins as well as in elucidating their mechanisms of action as therapeutic agents. Keywords Drug-protein binding haemoglobin myoglobin protoporphyrin IX red blood cells

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