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Probing protein-induced membrane fouling with in-situ attenuated total reflectance fourier transform infrared spectroscopy and multivariate curve resolution-alternating least squares.
Water Res. 2020 Jun 17; 183:116052.WR

Abstract

Proteins are one of the major contributors to membrane fouling. The interaction between proteins and the polymer membrane at the molecular level is essential for the alleviation/prevention of membrane fouling, but remains unclear. In this work, time-dependent in-situ attenuated total reflectance Fourier transform infrared spectroscopy is applied to investigate the interaction process between two model proteins, bovine serum albumin and lysozyme, and the poly(vinylidene fluoride) (PVDF) membrane. Multivariate curve resolution-alternating least squares is integrated with two-dimensional correlation spectroscopy analysis to resolve the membrane-induced conformational changes of proteins. The multivariate curve resolution-alternating least squares analysis reveals a two-step process in the protein-membrane interaction and provides the kinetics of the conformational transition, which aids the segmentation of the spectral dataset. By applying two-dimensional correlation spectroscopy analysis to different groups of the time-dependent spectra, the sequential order of the secondary structural changes of proteins is determined. The proteins initially undergo unfolding transition to a more open, less structured state, which appears to be triggered by the hydrophobic membrane surface. Afterwards, the proteins become aggregated with the high anti-parallel β-sheet content, aggravating the membrane fouling. The conformational transition process of proteins was also confirmed by the atomic force microscopic images and quartz crystal microbalance measurement. Overall, this work provides an in-depth understanding of the interaction between proteins and the membrane surface, which is helpful for the development of membrane anti-fouling strategies.

Authors+Show Affiliations

CAS Key Laboratory of Urban Pollutant Conversion, Department of Environmental Science and Engineering, University of Science and Technology of China, Hefei, 230026, China.School of Metallurgy and Environment, Central South University, Changsha, 410083, China.CAS Key Laboratory of Urban Pollutant Conversion, Department of Environmental Science and Engineering, University of Science and Technology of China, Hefei, 230026, China. Electronic address: hqyu@ustc.edu.cn.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

32622234

Citation

Liu, Xiao-Yang, et al. "Probing Protein-induced Membrane Fouling With In-situ Attenuated Total Reflectance Fourier Transform Infrared Spectroscopy and Multivariate Curve Resolution-alternating Least Squares." Water Research, vol. 183, 2020, p. 116052.
Liu XY, Chen W, Yu HQ. Probing protein-induced membrane fouling with in-situ attenuated total reflectance fourier transform infrared spectroscopy and multivariate curve resolution-alternating least squares. Water Res. 2020;183:116052.
Liu, X. Y., Chen, W., & Yu, H. Q. (2020). Probing protein-induced membrane fouling with in-situ attenuated total reflectance fourier transform infrared spectroscopy and multivariate curve resolution-alternating least squares. Water Research, 183, 116052. https://doi.org/10.1016/j.watres.2020.116052
Liu XY, Chen W, Yu HQ. Probing Protein-induced Membrane Fouling With In-situ Attenuated Total Reflectance Fourier Transform Infrared Spectroscopy and Multivariate Curve Resolution-alternating Least Squares. Water Res. 2020 Jun 17;183:116052. PubMed PMID: 32622234.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Probing protein-induced membrane fouling with in-situ attenuated total reflectance fourier transform infrared spectroscopy and multivariate curve resolution-alternating least squares. AU - Liu,Xiao-Yang, AU - Chen,Wei, AU - Yu,Han-Qing, Y1 - 2020/06/17/ PY - 2020/04/19/received PY - 2020/06/11/revised PY - 2020/06/12/accepted PY - 2020/7/6/pubmed PY - 2020/7/6/medline PY - 2020/7/5/entrez KW - Attenuated total reflectance fourier transform infrared spectroscopy KW - Membrane fouling KW - Multivariate curve resolution-alternating least squares analysis KW - Protein KW - Two-dimensional correlation spectroscopic analysis SP - 116052 EP - 116052 JF - Water research JO - Water Res. VL - 183 N2 - Proteins are one of the major contributors to membrane fouling. The interaction between proteins and the polymer membrane at the molecular level is essential for the alleviation/prevention of membrane fouling, but remains unclear. In this work, time-dependent in-situ attenuated total reflectance Fourier transform infrared spectroscopy is applied to investigate the interaction process between two model proteins, bovine serum albumin and lysozyme, and the poly(vinylidene fluoride) (PVDF) membrane. Multivariate curve resolution-alternating least squares is integrated with two-dimensional correlation spectroscopy analysis to resolve the membrane-induced conformational changes of proteins. The multivariate curve resolution-alternating least squares analysis reveals a two-step process in the protein-membrane interaction and provides the kinetics of the conformational transition, which aids the segmentation of the spectral dataset. By applying two-dimensional correlation spectroscopy analysis to different groups of the time-dependent spectra, the sequential order of the secondary structural changes of proteins is determined. The proteins initially undergo unfolding transition to a more open, less structured state, which appears to be triggered by the hydrophobic membrane surface. Afterwards, the proteins become aggregated with the high anti-parallel β-sheet content, aggravating the membrane fouling. The conformational transition process of proteins was also confirmed by the atomic force microscopic images and quartz crystal microbalance measurement. Overall, this work provides an in-depth understanding of the interaction between proteins and the membrane surface, which is helpful for the development of membrane anti-fouling strategies. SN - 1879-2448 UR - https://www.unboundmedicine.com/medline/citation/32622234/Probing_protein-induced_membrane_fouling_with_in-situ_attenuated_total_reflectance_fourier_transform_infrared_spectroscopy_and_multivariate_curve_resolution-alternating_least_squares L2 - https://linkinghub.elsevier.com/retrieve/pii/S0043-1354(20)30589-3 DB - PRIME DP - Unbound Medicine ER -
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