Structure study of recombinant RGD-hirudin by vibrational and circular dichroism spectroscopy.
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% beta-turn and 53% unordered structure, leaving no alpha-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 beta-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.
Liu
Xingang
X
Center of Analysis and Measurement, Fudan University, Shanghai, 200433, P.R.China.
Mo
Wei
W
Dai
Linsen
L
Yan
Xiaomin
X
Song
Houyan
H
D002942:Circular Dichroism / Q000379:methods*; D006629:Hirudins / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D017550:Spectroscopy, Fourier Transform Infrared; D013059:Spectrum Analysis, Raman
D006629:Hirudins; D010446:Peptide Fragments; D011994:Recombinant Proteins