Premium
Are the Interactions between Recombinant Prion Proteins and Polymeric Surfaces Related to the Hydrophilic/Hydrophobic Balance?
Author(s) -
Vrlinic Tjasa,
Debarnot Dominique,
Legeay Gilbert,
Coudreuse Arnaud,
El Moualij Benaissa,
Zorzi Willy,
PerretLiaudet Armand,
Quadrio Isabelle,
Mozetic Miran,
PoncinEpaillard Fabienne
Publication year - 2012
Publication title -
macromolecular bioscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.924
H-Index - 105
eISSN - 1616-5195
pISSN - 1616-5187
DOI - 10.1002/mabi.201100454
Subject(s) - recombinant dna , adhesion , chemistry , hydrophobic effect , fouling , coating , biophysics , protein aggregation , chemical engineering , biofouling , chromatography , polymer chemistry , biochemistry , membrane , organic chemistry , biology , engineering , gene
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).