Intermolecular forces between proteins and polymer films with relevance to filtration

被引:117
作者
Koehler, JA [1 ]
Ulbricht, M [1 ]
Belfort, G [1 ]
机构
[1] RENSSELAER POLYTECH INST,DEPT CHEM ENGN,HOWARD P ISERMANN DEPT CHEM ENGN,TROY,NY 12180
关键词
D O I
10.1021/la970010m
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
In order to understand the effects of protein fouling during ultrafiltration of biological fluids, we have investigated the molecular interactions between a thin polysulfone film and hen egg lysozyme with the surface forces apparatus (SFA). The normalized forces between the adsorbed protein layers and polymer films were measured below, at and above the pI of lysozyme, and compared with four different permeation fluxes obtained from ultrafiltration experiments. The intermolecular forces between two protein layers were also measured at the different pH values. Adsorption kinetics of lysozyme onto mica were also obtained. Buffer and lysozyme solutions at similar pH values and concentrations were filtered with 6 kD polysulfone membranes to obtain flux decline and hence fouling measurements. Hydrophobic membranes, such as polysulfone, exhibit extremely long-range attractive interactions (on the order of 1500-2000 Angstrom) with proteins such as lysozyme. Even in the presence of electrostatic repulsion at pH values above the isoelectric point of lysozyme (when both lysozyme and polysulfone were negatively charged), a long-range attractive interaction of around 210 mu N/m was observed. Such interactions were absent with measurements between adsorbed lysozyme-lysozyme layers. From these measurements, simple linear correlations were found relating the normalized forces to the fluxes from the ultrafiltration experiments. With respect to fouling, protein-protein and protein-polymer interactions are about equally important during ultrafiltration. This suggests that both the surface chemistry of the membrane and the solution conditions could be chosen to minimize fouling for specific protein solutions. Hence, as a result of this study, fouling of polysulfone membranes with lysozyme solutions can be reduced if (i) filtration is conducted at pH values above the pI oflysozyme (approximately 10.8) and (ii) the membranes are modified such that the long-range attractive interactions are reduced. These results support those from previous phenomenological studies on membrane filtration of protein solutions and are the first evidence relating intermolecular force interactions with macroscopic events in membrane fouling.
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收藏
页码:4162 / 4171
页数:10
相关论文
共 77 条
[11]   VERY LONG-RANGE ATTRACTIVE FORCES BETWEEN UNCHARGED HYDROCARBON AND FLUOROCARBON SURFACES IN WATER [J].
CLAESSON, PM ;
CHRISTENSON, HK .
JOURNAL OF PHYSICAL CHEMISTRY, 1988, 92 (06) :1650-1655
[12]   DIRECT MEASUREMENTS OF THE INTERACTION BETWEEN LAYERS OF INSULIN ADSORBED ON HYDROPHOBIC SURFACES [J].
CLAESSON, PM ;
ARNEBRANT, T ;
BERGENSTAHL, B ;
NYLANDER, T .
JOURNAL OF COLLOID AND INTERFACE SCIENCE, 1989, 130 (02) :457-466
[13]  
Creighton T. E., 1993, PROTEINS STRUCTURES, P266
[14]   MEASUREMENTS OF HYDROPHOBIC AND DLVO FORCES IN BUBBLE-SURFACE INTERACTIONS IN AQUEOUS-SOLUTIONS [J].
DUCKER, WA ;
XU, ZG ;
ISRAELACHVILI, JN .
LANGMUIR, 1994, 10 (09) :3279-3289
[15]   FORCES BETWEEN ALUMINA SURFACES IN SALT-SOLUTIONS - NON-DLVO FORCES AND THE IMPLICATIONS FOR COLLOIDAL PROCESSING [J].
DUCKER, WA ;
XU, Z ;
CLARKE, DR ;
ISRAELACHVILI, JN .
JOURNAL OF THE AMERICAN CERAMIC SOCIETY, 1994, 77 (02) :437-443
[16]   SORPTION OF HUMAN ALBUMIN AND ENDOTOXIN ON UNCHARGED AND CHARGED ULTRAFILTRATION MEMBRANES MADE FROM POLYSULFONE AND POLYETHERSULFONE [J].
DUPUTELL, D ;
STAUDE, E ;
WYSZYNSKI, D .
DESALINATION, 1994, 95 (01) :75-89
[17]   THE EFFECT OF PH AND IONIC ENVIRONMENT ON THE ULTRAFILTRATION OF PROTEIN SOLUTIONS WITH RETENTIVE MEMBRANES [J].
FANE, AG ;
FELL, CJD ;
SUKI, A .
JOURNAL OF MEMBRANE SCIENCE, 1983, 16 (DEC) :195-210
[18]   ULTRAFILTRATION OF PROTEIN SOLUTIONS THROUGH PARTIALLY PERMEABLE MEMBRANES - THE EFFECT OF ADSORPTION AND SOLUTION ENVIRONMENT [J].
FANE, AG ;
FELL, CJD ;
WATERS, AG .
JOURNAL OF MEMBRANE SCIENCE, 1983, 16 (DEC) :211-224
[19]   USE OF FOURIER-TRANSFORM INFRARED ATTENUATED TOTAL REFLECTANCE SPECTROSCOPY FOR THE STUDY OF SURFACE-ADSORPTION OF PROTEINS [J].
FU, FN ;
FULLER, MP ;
SINGH, BR .
APPLIED SPECTROSCOPY, 1993, 47 (01) :98-102
[20]  
GALLINET JP, 1993, EUR BIOPHYS J BIOPHY, V22, P195, DOI 10.1007/BF00185780