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Protein immobilization to polystyrene via long poly(ethylene lycol) chains
Author(s) -
Bergström Karin,
Holmberg Krister
Publication year - 1991
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260380817
Subject(s) - polystyrene , polymer chemistry , cationic polymerization , peg ratio , ethylene , chemistry , polymer , protein adsorption , copolymer , adsorption , ethylene glycol , organic chemistry , catalysis , finance , economics
Abstract Human albumin has been attached to 24‐hole polystyrene plates via branched poly(ethylene lycol) (PEG) spacer arms. A tetraepoxude of PEG of molecular weight (1.4–1.5) × 10 4 g/mol was reacted with the protein in solution allowing approximately one‐third of the oxirane rings to react. The protein conjugate was then coupled to the long, cationic polymer poly(ethylene imine) (PEI), and the protein‐PEG‐PEI adduct was subsequently adsorption to unmodified polystyrene. Since the protein is linked to the surface via long, hydrophilic and nonchargedchains, interactions between the biomolecule and the surface is minimized.