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High throughput synthesis and screening of new protein resistant surfaces for membrane filtration
Author(s) -
Zhou Mingyan,
Liu Hongwei,
Kilduff James E.,
Langer Robert,
Anderson Daniel G.,
Belfort Georges
Publication year - 2010
Publication title -
aiche journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.958
H-Index - 167
eISSN - 1547-5905
pISSN - 0001-1541
DOI - 10.1002/aic.12104
Subject(s) - filtration (mathematics) , membrane , monomer , bovine serum albumin , polymerization , sulfone , chromatography , adsorption , chemistry , polymer , protein adsorption , chemical engineering , materials science , combinatorial chemistry , polymer chemistry , organic chemistry , biochemistry , mathematics , engineering , statistics
A novel high throughput method for synthesis and screening of customized protein‐resistant surfaces was developed. This method is an inexpensive, fast, reproducible and scalable approach to synthesize and screen protein‐resistance surfaces appropriate for a specific feed. The method is illustrated here by combining a high throughput platform (HTP) approach together with our patented photo‐induced graft polymerization (PGP) method developed for facile modification of commercial poly(aryl sulfone) membranes. This new HTP‐PGP method was validated by comparison with our previous published results obtained using a bench‐scale filtration assay of six well‐studied monomers. Optimally‐performing surfaces for resisting a model protein, bovine serum albumin (BSA), were identified from a library of 66 monomers. Surfaces were prepared via graft polymerization onto poly(ether sulfone) (PES) membranes and were evaluated using a protein adsorption assay followed by pressure‐driven filtration. Bench‐scale verification was conducted for selected monomers using HTP‐PGP method; a good correlation with HTP‐PGP results was found. © 2009 American Institute of Chemical Engineers AIChE J, 2010