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Title: Molecular interactions between proteins and synthetic membrane polymer films

Abstract

To help understand the effects of protein adsorption on membrane filtration performance, we have measured the molecular interactions between cellulose acetate films and two proteins with different properties (ribonuclease A and human serum albumin) with a surface force apparatus. Comparison of forces between two protein layers with those between a protein layer and a cellulose acetate (CA) film shows that, at high pH, both proteins retained their native conformation on interacting with the CA film while at the isoelectric point (pI) or below the tertiary structure of proteins was disturbed. These measurements provide the first molecular evidence that disruption of protein tertiary structure could be responsible for the reduced permeation flows observed during membrane filtration of protein solutions and suggest that operating at high pH values away from the pI of proteins will reduce such fouling. 60 refs., 9 figs., 5 tabs.

Authors:
; ;  [1]
  1. Rensselaer Polytechnic Inst., Troy, NY (United States)
Publication Date:
Sponsoring Org.:
USDOE
OSTI Identifier:
45012
DOE Contract Number:  
FG02-90ER14114
Resource Type:
Journal Article
Journal Name:
Langmuir
Additional Journal Information:
Journal Volume: 11; Journal Issue: 4; Other Information: PBD: Apr 1995
Country of Publication:
United States
Language:
English
Subject:
55 BIOLOGY AND MEDICINE, BASIC STUDIES; 36 MATERIALS SCIENCE; 40 CHEMISTRY; PROTEINS; FILTRATION; EXPERIMENTAL DATA; MEMBRANES; MEMBRANE TRANSPORT; POLYMERS; CELLULOSE ESTERS; FILMS; CONFIGURATION INTERACTION

Citation Formats

Pincet, F, Perez, E, and Belfort, G. Molecular interactions between proteins and synthetic membrane polymer films. United States: N. p., 1995. Web. doi:10.1021/la00004a031.
Pincet, F, Perez, E, & Belfort, G. Molecular interactions between proteins and synthetic membrane polymer films. United States. https://doi.org/10.1021/la00004a031
Pincet, F, Perez, E, and Belfort, G. 1995. "Molecular interactions between proteins and synthetic membrane polymer films". United States. https://doi.org/10.1021/la00004a031.
@article{osti_45012,
title = {Molecular interactions between proteins and synthetic membrane polymer films},
author = {Pincet, F and Perez, E and Belfort, G},
abstractNote = {To help understand the effects of protein adsorption on membrane filtration performance, we have measured the molecular interactions between cellulose acetate films and two proteins with different properties (ribonuclease A and human serum albumin) with a surface force apparatus. Comparison of forces between two protein layers with those between a protein layer and a cellulose acetate (CA) film shows that, at high pH, both proteins retained their native conformation on interacting with the CA film while at the isoelectric point (pI) or below the tertiary structure of proteins was disturbed. These measurements provide the first molecular evidence that disruption of protein tertiary structure could be responsible for the reduced permeation flows observed during membrane filtration of protein solutions and suggest that operating at high pH values away from the pI of proteins will reduce such fouling. 60 refs., 9 figs., 5 tabs.},
doi = {10.1021/la00004a031},
url = {https://www.osti.gov/biblio/45012}, journal = {Langmuir},
number = 4,
volume = 11,
place = {United States},
year = {Sat Apr 01 00:00:00 EST 1995},
month = {Sat Apr 01 00:00:00 EST 1995}
}