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High Temperature Material Processes: An International Quarterly of High-Technology Plasma Processes
SJR: 0.19 SNIP: 0.341 CiteScore™: 0.43

ISSN Print: 1093-3611
ISSN Online: 1940-4360

High Temperature Material Processes: An International Quarterly of High-Technology Plasma Processes

DOI: 10.1615/HighTempMatProc.v8.i2.160
pages 321-330

COVALENT CROSS-LINKING OF PROTEINS BY A NON-THERMAL PLASMA PROCESS

B. Dodet
Service Electrotechnique et Electronique Industrielle, SUPELEC, 91192 Gif-sur-Yvette Cedex, France
D. Beggar
Institut de Genetique et Microbiologie, UMR C8621 CNRS-UPS, 91405 Orsay Cedex, France
E. Odic
Equipe Decharges Electriques et Environnement, Laboratoire de Physique des Gaz et des Plasmas, Universite Paris-Sud / CNRS Supelec, plateau de Moulon, 91192 Gif-sur-Yvette Cedex, FRANCE.
S. Salamitou
Institut de Genetique et Microbiologie, UMR C8621 CNRS-UPS, 91405 Orsay Cedex, France
F. Le Hegarat
Institut de Genetique et Microbiologie, UMR C8621 du CNRS, Universite Paris-Sud, 91405 Orsay Cedex, France
G. Leblon
Institut de Genetique et Microbiologie, UMR C8621 CNRS-UPS, 91405 Orsay Cedex, France
A. Goldman
Equipe Decharges Electriques et Environnement, Laboratoire de Physique des Gaz et des Plasmas, UMR 8578 du CNRS, Supelec, 91192 Gif-sur-Yvette Cedex, France
M. Goldman
Equipe Decharges Electriques et Environnement, Laboratoire de Physique des Gaz et des Plasmas, UMR 8578 du CNRS, Supelec, 91192 Gif-sur-Yvette Cedex, France

ABSTRACT

An atmospheric pressure, room temperature (18-25 °C) gas discharge process has been investigated for its ability to elicit protein covalent cross-linking leading to oligomers. A practical application of such technique is to improve the stability of heat sensitive proteins of medical interest. A non-thermal plasma can be produced in transient filamentary discharge channels taking place in an atmospheric pressure dielectric barrier discharge reactor. The proteins are submitted to the discharge reactor effluents in an aqueous solution, consisting of lysozyme (14 kD) aqueous solutions (25 mg/ml). The protein solution is split up into 10 μl droplets deposited on a target surface in order to increase the gas/liquid exchange surface. After the plasma treatment, the proteins cross-linking reaction was ascertained by the visualization of protein bands on SDS-polyacrylamide gels corresponding to dimers (28 kD) and trimers (42 kD) of lysozyme. The intermolecular bonds were found to be covalent since the same migration bands were obtained in drastic denaturing conditions (disrupting hydrogen and Van der Waals intermolecular bonds). Under specific operating conditions, approximately 20 % of the total protein present is converted into dimers and trimers after only 5 minutes treatment. The influence, on the cross-linking efficiency, of different parameters (feed gas composition, exposure duration and solution composition) is discussed in the paper. First results suggest a possible biological activity of the cross-linked dimers.


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