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2000
Volume 13, Issue 1
  • ISSN: 0929-8665
  • E-ISSN: 1875-5305

Abstract

The secondary structure of a new type of recombinant RGD-hirudin, which has the activities of anti-thrombin and anti-platelet aggregation, has been studied by Fourier transform infrared spectroscopy (FT-IR), Raman spectroscopy and circular dichroism (CD) methods. The distribution of various secondary structure elements was determined using only a very small amount of sample protein. It was found that the recombinant RGD-hirudin contains about 26% extended chain, 21% β-turn and 53% unordered structure, leaving no α-helix. The results showed that the regular secondary structure of recombinant RGD-hirudin is increased compared with wild-type hirudin. The RGD segment that is located at the end of a long arm of a β-sheet is thought to play an important role in the additional function of anti-platelet aggregation. Throughout the experiments, FT-IR, Raman spectroscopy and CD generated mutually reinforcing results.

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/content/journals/ppl/10.2174/092986606774502135
2006-01-01
2025-05-23
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  • Article Type:
    Research Article
Keyword(s): CD; FT-IR; Raman spectroscopy; Recombinant RGD-hirudin; secondary structure
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