NDLI: The protein modification in the Electron Beam Plasmachemical Reactor with the aerosol reaction bulk

Content Provider	IEEE Xplore Digital Library
Author	Vasilieva, T. Mahir, A.
Copyright Year	2008
Description	Author affiliation: Moscow Inst. of Phys. & Technol., Moscow (Vasilieva, T.; Mahir, A.)
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 $H_{2}O-EBP$ 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 $H_{2}O-EBP.$ This peptide is likely to be responsible for 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.
Starting Page	1
Ending Page	1
File Size	35329
Page Count	1
File Format	PDF
ISBN	9781424419296
ISSN	07309244
DOI	10.1109/PLASMA.2008.4591146
Language	English
Publisher	Institute of Electrical and Electronics Engineers, Inc. (IEEE)
Publisher Date	2008-06-15
Publisher Place	Germany
Access Restriction	Subscribed
Rights Holder	Institute of Electrical and Electronics Engineers, Inc. (IEEE)
Content Type	Text
Resource Type	Article
Subject	Atomic and Molecular Physics, and Optics Condensed Matter Physics Electrical and Electronic Engineering

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