A Caltech Library Service

Intermolecular Forces between a Protein and a Hydrophilic Modified Polysulfone Film with Relevance to Filtration

Koehler, Jeffrey A. and Ulbricht, Mathias and Belfort, Georges (2000) Intermolecular Forces between a Protein and a Hydrophilic Modified Polysulfone Film with Relevance to Filtration. Langmuir, 16 (26). pp. 10419-10427. ISSN 0743-7463. doi:10.1021/la000593r.

Full text is not posted in this repository. Consult Related URLs below.

Use this Persistent URL to link to this item:


Correlations between intermolecular forces and ultrafiltration measurements for a thin polysulfone film and membranes modified for increased hydrophilicity by graft polymerization of 2-hydroxyethyl methacrylate and a model protein (hen egg-white lysozyme, Lz) suggest that altering either the chemistry of the polymer surface or the solution conditions should lead to a minimization of protein adhesion and hence fouling for a specific protein/polymer combination. Using the surface forces apparatus, normalized adhesion forces were measured below, at and above the pI of Lz, and compared with corresponding permeation flux ratios from ultrafiltration experiments. Simple exponential correlations were obtained relating the normalized adhesion forces to several different permeation flux ratios. Also, the amount of protein adsorbed onto the membrane from solution during filtration was linearly related to the adhesion force through the choice of solution pH. The correlations imply that protein−polymer adhesive interactions are important during ultrafiltration. The results obtained for both a hydrophilic and a hydrophobic surface were compared. The hydrophilic surface exhibited lower contact angles, reduced adhesion forces, reduced adsorbed amount, and most importantly, reduced protein fouling. Long range attraction between adsorbed protein and hydrophobic polysulfone films was absent with the hydrophilic films. The results provide a fundamental molecular basis to the widely reported and observed phenomenon that hydrophilic membranes are known to foul less than hydrophobic ones during membrane filtration of protein solutions.

Item Type:Article
Related URLs:
URLURL TypeDescription
Additional Information:© 2000 American Chemical Society. Received 3 April 2000. Published online 18 November 2000. Published in print 1 December 2000. We acknowledge the support of the U.S. Department of Energy, Basic Chemical Science Division (Grant No. DE-FG02-90ER14114). Amicon Division (formally W.R. Grace), Millipore Corp., Danverse, MA, donated the TCF-2 membrane cell. Mr. Ole Olson, Danish Separation Systems AS (formally Dow Danske), Nakskov, Denmark, donated the gr81pp polysulfone membranes. The coordinates for lysozyme were obtained from the Protein Data Bank (entry 1HEL by Wilson et al.63).
Funding AgencyGrant Number
Department of Energy (DOE)DE-FG02-90ER14114
Issue or Number:26
Record Number:CaltechAUTHORS:20170427-101139528
Persistent URL:
Official Citation:Intermolecular Forces between a Protein and a Hydrophilic Modified Polysulfone Film with Relevance to Filtration Jeffrey A. Koehler, Mathias Ulbricht, and Georges Belfort Langmuir 2000 16 (26), 10419-10427 DOI: 10.1021/la000593r
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:76995
Deposited By: Ruth Sustaita
Deposited On:27 Apr 2017 17:27
Last Modified:15 Nov 2021 17:04

Repository Staff Only: item control page