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Purification and Refolding to Amyloid Fibrils of (His)6-tagged Recombinant Shadoo Protein Expressed as Inclusion Bodies in E. coli
Published on: December 19, 2015
Are the interactions between recombinant prion proteins and polymeric surfaces related to the hydrophilic/hydrophobic
Tjasa Vrlinic1, Dominique Debarnot, Gilbert Legeay
1LUNAM Université, UMR Université du Maine-CNRS n° 6283, Institut des Molécules et Matériaux du Mans-Département, Av. O. Messiaen, 72085 Le Mans, France.
Abstract:
New non-fouling tubes are developed and their influence on the adhesion of neuroproteins is studied. Recombinant prion proteins are considered as a single component representative of hydrophobic proteins. Samples are stored for 24 h at 4 °C in tubes coated with two different coatings: poly(N-isopropylacrylamide) as a hydrophilic surface and a plasma-fluorinated coating as a hydrophobic one. The protein adhesion is monitored by ELISA tests, XPS and confocal microscopy. It appears that the highest recovery of recombinant prion protein in the liquid phase is obtained with the hydrophilic surface while the hydrophobic character of the storage tube induces an important amount of biological loss. However, the recovery is not complete even for tubes coated with poly(N-isopropylacrylamide).
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