Membrane protein extraction and purification using styrene–maleic acid (SMA) copolymer: effect of variations in polymer structure

Research output: Contribution to journalArticlepeer-review

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Membrane protein extraction and purification using styrene–maleic acid (SMA) copolymer: effect of variations in polymer structure. / Morrison, Kerrie; Akram, Aneel; Mathews, Ashlyn; Khan, Zoeya; Patel, Jaimin; Zhou, Chumin; Hardy, David; Moore-Kelly, Charles; Patel, Roshani; Obida, Victor; Knowles, Timothy; Javed, Massod-ul-hassan; Chmel, Nikola; Dafforn, Timothy; Rothnie, Alice.

In: Biochemical Journal, Vol. 473, No. 23, 25.11.2016, p. 4349-4360.

Research output: Contribution to journalArticlepeer-review

Harvard

Morrison, K, Akram, A, Mathews, A, Khan, Z, Patel, J, Zhou, C, Hardy, D, Moore-Kelly, C, Patel, R, Obida, V, Knowles, T, Javed, M, Chmel, N, Dafforn, T & Rothnie, A 2016, 'Membrane protein extraction and purification using styrene–maleic acid (SMA) copolymer: effect of variations in polymer structure', Biochemical Journal, vol. 473, no. 23, pp. 4349-4360. https://doi.org/10.1042/BCJ20160723

APA

Morrison, K., Akram, A., Mathews, A., Khan, Z., Patel, J., Zhou, C., Hardy, D., Moore-Kelly, C., Patel, R., Obida, V., Knowles, T., Javed, M., Chmel, N., Dafforn, T., & Rothnie, A. (2016). Membrane protein extraction and purification using styrene–maleic acid (SMA) copolymer: effect of variations in polymer structure. Biochemical Journal, 473(23), 4349-4360. https://doi.org/10.1042/BCJ20160723

Vancouver

Author

Morrison, Kerrie ; Akram, Aneel ; Mathews, Ashlyn ; Khan, Zoeya ; Patel, Jaimin ; Zhou, Chumin ; Hardy, David ; Moore-Kelly, Charles ; Patel, Roshani ; Obida, Victor ; Knowles, Timothy ; Javed, Massod-ul-hassan ; Chmel, Nikola ; Dafforn, Timothy ; Rothnie, Alice. / Membrane protein extraction and purification using styrene–maleic acid (SMA) copolymer: effect of variations in polymer structure. In: Biochemical Journal. 2016 ; Vol. 473, No. 23. pp. 4349-4360.

Bibtex

@article{24d9668ebfb34c8a90f7de5c91376ec6,
title = "Membrane protein extraction and purification using styrene–maleic acid (SMA) copolymer: effect of variations in polymer structure",
abstract = "The use of styrene–maleic acid (SMA) copolymers to extract and purify transmembrane proteins, while retaining their native bilayer environment, overcomes many of the disadvantages associated with conventional detergent-based procedures. This approach has huge potential for the future of membrane protein structural and functional studies. In this investigation, we have systematically tested a range of commercially available SMA polymers, varying in both the ratio of styrene and maleic acid and in total size, for the ability to extract, purify and stabilise transmembrane proteins. Three different membrane proteins (BmrA, LeuT and ZipA), which vary in size and shape, were used. Our results show that several polymers, can be used to extract membrane proteins, comparably to conventional detergents. A styrene:maleic acid ratio of either 2:1 or 3:1, combined with a relatively small average molecular mass (7.5–10 kDa), is optimal for membrane extraction, and this appears to be independent of the protein size, shape or expression system. A subset of polymers were taken forward for purification, functional and stability tests. Following a one-step affinity purification, SMA 2000 was found to be the best choice for yield, purity and function. However, the other polymers offer subtle differences in size and sensitivity to divalent cations that may be useful for a variety of downstream applications.",
author = "Kerrie Morrison and Aneel Akram and Ashlyn Mathews and Zoeya Khan and Jaimin Patel and Chumin Zhou and David Hardy and Charles Moore-Kelly and Roshani Patel and Victor Obida and Timothy Knowles and Massod-ul-hassan Javed and Nikola Chmel and Timothy Dafforn and Alice Rothnie",
year = "2016",
month = nov,
day = "25",
doi = "10.1042/BCJ20160723",
language = "English",
volume = "473",
pages = "4349--4360",
journal = "Biochem J",
issn = "0264-6021",
publisher = "Portland Press",
number = "23",

}

RIS

TY - JOUR

T1 - Membrane protein extraction and purification using styrene–maleic acid (SMA) copolymer: effect of variations in polymer structure

AU - Morrison, Kerrie

AU - Akram, Aneel

AU - Mathews, Ashlyn

AU - Khan, Zoeya

AU - Patel, Jaimin

AU - Zhou, Chumin

AU - Hardy, David

AU - Moore-Kelly, Charles

AU - Patel, Roshani

AU - Obida, Victor

AU - Knowles, Timothy

AU - Javed, Massod-ul-hassan

AU - Chmel, Nikola

AU - Dafforn, Timothy

AU - Rothnie, Alice

PY - 2016/11/25

Y1 - 2016/11/25

N2 - The use of styrene–maleic acid (SMA) copolymers to extract and purify transmembrane proteins, while retaining their native bilayer environment, overcomes many of the disadvantages associated with conventional detergent-based procedures. This approach has huge potential for the future of membrane protein structural and functional studies. In this investigation, we have systematically tested a range of commercially available SMA polymers, varying in both the ratio of styrene and maleic acid and in total size, for the ability to extract, purify and stabilise transmembrane proteins. Three different membrane proteins (BmrA, LeuT and ZipA), which vary in size and shape, were used. Our results show that several polymers, can be used to extract membrane proteins, comparably to conventional detergents. A styrene:maleic acid ratio of either 2:1 or 3:1, combined with a relatively small average molecular mass (7.5–10 kDa), is optimal for membrane extraction, and this appears to be independent of the protein size, shape or expression system. A subset of polymers were taken forward for purification, functional and stability tests. Following a one-step affinity purification, SMA 2000 was found to be the best choice for yield, purity and function. However, the other polymers offer subtle differences in size and sensitivity to divalent cations that may be useful for a variety of downstream applications.

AB - The use of styrene–maleic acid (SMA) copolymers to extract and purify transmembrane proteins, while retaining their native bilayer environment, overcomes many of the disadvantages associated with conventional detergent-based procedures. This approach has huge potential for the future of membrane protein structural and functional studies. In this investigation, we have systematically tested a range of commercially available SMA polymers, varying in both the ratio of styrene and maleic acid and in total size, for the ability to extract, purify and stabilise transmembrane proteins. Three different membrane proteins (BmrA, LeuT and ZipA), which vary in size and shape, were used. Our results show that several polymers, can be used to extract membrane proteins, comparably to conventional detergents. A styrene:maleic acid ratio of either 2:1 or 3:1, combined with a relatively small average molecular mass (7.5–10 kDa), is optimal for membrane extraction, and this appears to be independent of the protein size, shape or expression system. A subset of polymers were taken forward for purification, functional and stability tests. Following a one-step affinity purification, SMA 2000 was found to be the best choice for yield, purity and function. However, the other polymers offer subtle differences in size and sensitivity to divalent cations that may be useful for a variety of downstream applications.

U2 - 10.1042/BCJ20160723

DO - 10.1042/BCJ20160723

M3 - Article

VL - 473

SP - 4349

EP - 4360

JO - Biochem J

JF - Biochem J

SN - 0264-6021

IS - 23

ER -