DocumentCode :
2444187
Title :
The protein modification in the Electron Beam Plasmachemical Reactor with the aerosol reaction bulk
Author :
Vasilieva, Tatiana ; Mahir, Abdul
Author_Institution :
Moscow Inst. of Phys. & Technol., Moscow
fYear :
2008
fDate :
15-19 June 2008
Firstpage :
1
Lastpage :
1
Abstract :
Summary form only given. The original Electron Beam Plasmachemical Reactor for the controllable biomacromolecules modification, production of biomaterials with desired biological properties and functional supramolecular architectures synthesis was designed. The Electron Beam Plasma (EBP) was generated inside the reaction chamber by injecting an electron beam into a gas filling the chamber, the range of the gas pressure being Pm ~ 5-50 Ton- depending on the kind of the gas. Within the pressure range mentioned above the EBP is strongly non-equilibrium and chemically active even at low temperature. The novel approach was applied to the controllable protein modification for the production of novel effective human platelet aggregation inhibitors, the blood protein fibrin- monomer (FM) being used as original substance. The dispersed powder of the native FM was introduced into the plasma cloud and the aerosol reaction bulk was formed inside the chamber. The FM was treated in plasma of helium or water vapor. The water-soluble products of the FM appropriately treated by the EBP of both helium and water vapor (moderate radiation dose) were found to decrease the platelet aggregation down to ap33-35 % in vitro at concentrations 1times10-4-1 mg/ml, treatment in the H2O-EBP being more effective than that in He-EBP. The EBR-treatment was found to cause the partial destruction of peptide -CO-NH- bounds in the primary fibrin-monomer structure and the oxidation of disulfide bounds stabilizing tertiary peptides structure. The EBP-rrearment reduced the amount of some amino acids forming the primary protein structure. The percentages of lysine, cystine, tyrosine and phenylalanine were found to be reduced significantly (down to 2 times with respect to the native FM). The peak corresponding to the elution time 12,3 min was observed at the exclusion chromatograms of the FM modified in the He-EBP and in the H2O-EBP. This peptide is likely to be responsible f- - or the inhibiting of the platelet aggregation. Our previous studies showed the combination of plasma-chemical processes, the fast electrons bombardment, and X-ray irradiation to be responsible for the modification of the original biomaterials but the effects appearing due to the plasmachemical modification predominate.
Keywords :
aerosols; chemical reactors; macromolecules; molecular biophysics; proteins; solubility; H2O-EBP; He-EBP; aerosol reaction bulk; amino acids; biomaterials; blood protein fibrin-monomer; controllable biomacromolecules modification; controllable protein modification; desired biological properties; disulfide oxidation; functional supramolecular architectures synthesis; helium; human platelet aggregation inhibitors; original electron beam plasmachemical reactor; peptide -CO-NH- bounds; primary fibrin-monomer structure; protein structure; reaction chamber; water vapor; water-soluble products; Aerosols; Amino acids; Electron beams; Inductors; Peptides; Plasma chemistry; Plasma properties; Plasma temperature; Production; Proteins;
fLanguage :
English
Publisher :
ieee
Conference_Titel :
Plasma Science, 2008. ICOPS 2008. IEEE 35th International Conference on
Conference_Location :
Karlsruhe
ISSN :
0730-9244
Print_ISBN :
978-1-4244-1929-6
Electronic_ISBN :
0730-9244
Type :
conf
DOI :
10.1109/PLASMA.2008.4591146
Filename :
4591146
Link To Document :
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